DB code: T00089

RLCP classification 5.161.586000.968 : Elimination
6.30.83700.5070 : Double-bonded atom exchange
8.12111.711000.5510 : Isomerization
5.14.3250000.5471 : Elimination
4.1164.693000.5470 : Addition
8.11211.912000.5510 : Isomerization
6.40.477300.5510 : Double-bonded atom exchange
CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
3.40.50.1100 : Rossmann fold Catalytic domain
3.40.50.1100 : Rossmann fold Catalytic domain
E.C. 4.2.1.20
CSA 1a50 1geq
M-CSA 1a50 1geq
MACiE

CATH domain Related DB codes (homologues)
3.20.20.70 : TIM Barrel S00215 S00217 S00218 S00219 S00532 S00198 S00220 S00745 S00537 S00538 S00539 S00826 S00841 S00235 S00239 S00240 S00243 S00244 S00199 S00200 S00201 S00221 S00222 S00847 S00224 S00225 S00226 D00014 D00029 M00141 T00015 T00239 D00664 D00665 D00804 D00863
3.40.50.1100 : Rossmann fold D00264 T00088

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q8U094 Tryptophan synthase alpha chain
EC 4.2.1.20
NP_579434.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
PF00290 (Trp_syntA)
[Graphical View]
P00929 Tryptophan synthase alpha chain
EC 4.2.1.20
NP_460686.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PF00290 (Trp_syntA)
[Graphical View]
Q8U093 Tryptophan synthase beta chain 1
EC 4.2.1.20
NP_579435.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
PF00291 (PALP)
[Graphical View]
Q8U0J5 Tryptophan synthase beta chain 2
EC 4.2.1.20
NP_579321.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
PF00291 (PALP)
[Graphical View]
P0A2K1 Tryptophan synthase beta chain
EC 4.2.1.20
NP_460685.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PF00291 (PALP)
[Graphical View]

KEGG enzyme name
tryptophan synthase
L-tryptophan synthetase
indoleglycerol phosphate aldolase
tryptophan desmolase
tryptophan synthetase
L-serine hydro-lyase (adding indoleglycerol-phosphate)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q8U094 TRPA_PYRFU L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. Tetramer of two alpha and two beta chains (By similarity).
P00929 TRPA_SALTY L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. Tetramer of two alpha and two beta chains.
Q8U093 TRPB1_PYRFU L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. Tetramer of two alpha and two beta chains (By similarity). Pyridoxal phosphate (By similarity).
Q8U0J5 TRPB2_PYRFU L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. Tetramer of two alpha and two beta chains (By similarity). Pyridoxal phosphate (By similarity).
P0A2K1 TRPB_SALTY L-serine + 1-C-(indol-3-yl)glycerol 3- phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H(2)O. Tetramer of two alpha and two beta chains. Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00400 Phenylalanine, tyrosine and tryptophan biosynthesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C99999 C00065 C03506 C00078 C00118 C00001 C00463 I00043 I00182 I00171 I00183 I00181
E.C.
Compound Pyridoxal phosphate Monovalent ion L-Serine 1-(Indol-3-yl)glycerol 3-phosphate L-Tryptophan D-Glyceraldehyde 3-phosphate H2O Indole External aldimine intermediate (initial stage:PLP-L-Ser) Quinonoid intermediate (PLP-Ser) Aminoacrylate intermediate (PLP-dehydroAla) Quinonoid intermediate (PLP-Trp) External aldimine intermeidate (final stage:PLP-L-TRP)
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion organic ion amino acids,carbohydrate aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amino acids,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms) carbohydrate,phosphate group/phosphate ion H2O
ChEBI 18405
 18405
 		17115
 33384
 17115
 33384
 		51793
 51793
 		16828
 57912
 16828
 57912
 		29052
 29052
 		15377
 15377
PubChem 1051
 1051
 		5951
 6857581
 5951
 6857581
 		444150
 444150
 		6305
 6923516
 6305
 6923516
 		439168
 439168
 		22247451
 962
 22247451
 962
1geqA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1geqB Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a50A Unbound Unbound Unbound Analogue:FIP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5aA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5bA Unbound Unbound Unbound Bound:IGP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5sA Unbound Unbound Unbound Analogue:FIP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1beuA Unbound Unbound Unbound Analogue:IPL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bksA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c29A Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c8vA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c9dA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cw2A Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cx9A Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fuyA Unbound Unbound Unbound Analogue:FIP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k3uA Unbound Unbound Unbound Analogue:IAD Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7eA Unbound Unbound Unbound Analogue:IAG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7fA Unbound Unbound Unbound Analogue:IAV Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8xA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8yA Unbound Unbound Unbound Unbound Unbound Bound:13P Unbound Unbound Unbound Unbound Unbound Unbound
1k8zA Unbound Unbound Unbound Analogue:IAG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfbA Unbound Unbound Unbound Bound:IGP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfcA Unbound Unbound Unbound Analogue:IPL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfeA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfjA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfkA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qopA Unbound Unbound Unbound Analogue:IPL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qoqA Unbound Unbound Unbound Bound:IGP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttpA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttqA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ubsA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1wsyA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2trsA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tsyA Unbound Unbound Unbound Unbound Unbound Bound:G3P Unbound Unbound Unbound Unbound Unbound Unbound
2tysA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2wsyA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a50B01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5aB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5bB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5sB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLP-SER Unbound Unbound
1beuB01 Analogue:PLS Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLS Unbound Unbound Unbound Unbound
1bksB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c29B01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c8vB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c9dB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cw2B01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cx9B01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fuyB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k3uB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7eB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7fB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8xB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8yB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8zB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfbB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfcB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfeB01 Analogue:PLS Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLS Unbound Unbound Unbound Unbound
1kfjB01 Analogue:PLS Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLS Unbound Unbound Unbound Unbound
1kfkB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qopB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qoqB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttpB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttqB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ubsB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLP-SER Unbound Unbound Unbound Unbound
1wsyB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2trsB01 Analogue:PLS Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLS Unbound Unbound Unbound Unbound
2tsyB01 Analogue:PLS Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLS Unbound Unbound Unbound Unbound
2tysB01 Analogue:PLT Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PLT
2wsyB01 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a50B02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5aB02 Unbound Bound:__K Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5bB02 Unbound Bound:__K Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a5sB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1beuB02 Unbound Bound:__K Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bksB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c29B02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c8vB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c9dB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cw2B02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cx9B02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fuyB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k3uB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7eB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k7fB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8xB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8yB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1k8zB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfbB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfcB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfeB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfjB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kfkB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qopB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qoqB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttpB02 Unbound Bound:_CS Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ttqB02 Unbound Bound:__K Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ubsB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1wsyB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2trsB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tsyB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2tysB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2wsyB02 Unbound Bound:_NA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00929 & PDB;1bks, 1qoq, 1ttp, 1ttq

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1geqA GLU 36;ASP 47; invisible 167-173
1geqB GLU 36;ASP 47;THR 168 invisible 170-172
1a50A GLU 49;ASP 60;THR 183
1a5aA GLU 49; ; mutant D60N, invisible 177-189
1a5bA GLU 49; ; mutant D60N, invisible 177-195
1a5sA GLU 49;ASP 60;THR 183
1beuA GLU 49; ; mutant D60N, invisible 177-191
1bksA GLU 49;ASP 60; invisible 178-189
1c29A GLU 49;ASP 60;THR 183
1c8vA GLU 49;ASP 60;THR 183
1c9dA GLU 49;ASP 60;THR 183
1cw2A GLU 49;ASP 60;THR 183
1cx9A GLU 49;ASP 60;THR 183
1fuyA GLU 49;ASP 60;THR 183
1k3uA GLU 49;ASP 60;THR 183
1k7eA GLU 49;ASP 60;THR 183
1k7fA GLU 49;ASP 60; invisible 179-192
1k8xA GLU 49;ASP 60; mutant T183V, invisible 178-195
1k8yA GLU 49;ASP 60; mutant S178P, invisible 179-191
1k8zA GLU 49;ASP 60; mutant S178P, invisible 179-189
1kfbA GLU 49;ASP 60; mutant T183V, invisivle 180-192
1kfcA GLU 49;ASP 60; mutant T183V, invisivle 179-192
1kfeA GLU 49;ASP 60; mutant T183V, invisivle 178-193
1kfjA GLU 49;ASP 60; invisible 178-191
1kfkA GLU 49;ASP 60; invisible 178-193
1qopA GLU 49;ASP 60;THR 183
1qoqA GLU 49;ASP 60; invisible 179-192
1ttpA GLU 49;ASP 60; invisible 178-189
1ttqA GLU 49;ASP 60; invisible 178-189
1ubsA GLU 49;ASP 60; invisible 181-191
1wsyA GLU 49;ASP 60; invisible 178-191
2trsA GLU 49;ASP 60;THR 183
2tsyA GLU 49;ASP 60;THR 183
2tysA GLU 49;ASP 60; invisible 179-191
2wsyA GLU 49; ; invisible 54-62, 177-195
1a50B01 LYS 87;GLU 109 LYS 87(PLP binding)
1a5aB01 LYS 87;GLU 109 LYS 87(PLP binding)
1a5bB01 LYS 87;GLU 109 LYS 87(PLP binding)
1a5sB01 LYS 87;GLU 109 LYS 87(PLP binding)
1beuB01 LYS 87;GLU 109 LYS 87(PLP binding)
1bksB01 LYS 87;GLU 109 LYS 87(PLP binding)
1c29B01 LYS 87;GLU 109 LYS 87(PLP binding)
1c8vB01 LYS 87;GLU 109 LYS 87(PLP binding)
1c9dB01 LYS 87;GLU 109 LYS 87(PLP binding)
1cw2B01 LYS 87;GLU 109 LYS 87(PLP binding)
1cx9B01 LYS 87;GLU 109 LYS 87(PLP binding)
1fuyB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k3uB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k7eB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k7fB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k8xB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k8yB01 LYS 87;GLU 109 LYS 87(PLP binding)
1k8zB01 LYS 87;GLU 109 LYS 87(PLP binding)
1kfbB01 LYS 87;GLU 109 LYS 87(PLP binding)
1kfcB01 LYS 87;GLU 109 LYS 87(PLP binding)
1kfeB01 LYS 87;GLU 109 LYS 87(PLP binding)
1kfjB01 LYS 87;GLU 109 LYS 87(PLP binding)
1kfkB01 LYS 87;GLU 109 LYS 87(PLP binding)
1qopB01 LYS 87;GLU 109 LYS 87(PLP binding)
1qoqB01 LYS 87;GLU 109 LYS 87(PLP binding)
1ttpB01 LYS 87;GLU 109 LYS 87(PLP binding)
1ttqB01 LYS 87;GLU 109 LYS 87(PLP binding)
1ubsB01 ;GLU 109 mutant K87T
1wsyB01 LYS 87;GLU 109 LYS 87(PLP binding)
2trsB01 ;GLU 109 mutant K87T
2tsyB01 ;GLU 109 mutant K87T
2tysB01 ;GLU 109 mutant K87T
2wsyB01 LYS 87;GLU 109 LYS 87(PLP binding)
1a50B02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1a5aB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1a5bB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1a5sB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1beuB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1bksB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1c29B02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1c8vB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1c9dB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1cw2B02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1cx9B02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1fuyB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding) mutant A169L;C170W
1k3uB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1k7eB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1k7fB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1k8xB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1k8yB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1k8zB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1kfbB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1kfcB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1kfeB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1kfjB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1kfkB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1qopB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1qoqB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1ttpB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1ttqB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1ubsB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
1wsyB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
2trsB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
2tsyB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
2tysB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)
2wsyB02 HIS 86;ASP 305 GLY 232;PHE 306;SER 308(Monovalent ion binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.28-30
[5]
Fig.15, Fig.16, Fig.17, Fig.18, Fig.19, p.128-151
[11]
Scheme I, Scheme II, p.1185 9
[12]
Scheme I, Fig.1, p.3836-3838 9
[16]
Scheme I, p.8733 8
[17]
FIG. 1, p.14930-14931 8
[21]
Scheme 1, p.9473-9475 9
[22]
SCHEME I, p.17336-17337 5
[25]
Scheme 1, p.7384 11
[26]
Scheme 1 11
[29]
Scheme 1A, Fig.11, p.7674-7678
[32]
Figure 1 10
[34]
Scheme 1 10
[35]
Scheme 1B 5
[36]
FIGURE 2 5
[38]
SCHEME 1, p.8555 2
[39]
SCHEME 1, p.33252 7
[42]
Fig.1, p.12672-12673 2
[43]
p.16479
[44]
Scheme 1, p.7134-7141 10
[45]
Scheme 1, p.7127-7129 6
[46]
SCHEME 1, p.31191-31194 9
[48]
Fig.3, Fig.9, p.118-124, p.127-132
[52]
Scheme 1, p.7430-7432 6
[54]
Scheme 1 7
[55]
Scheme 1, Scheme 2, p.9998-10000 6
[59]
Fig.1

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 89034326
PubMed ID 3053720
Journal J Biol Chem
Year 1988
Volume 263
Pages 17857-71
Authors Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR
Title Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
Related PDB
Related UniProtKB P00929 P0A2K1
[2]
Resource
Comments
Medline ID
PubMed ID 1366510
Journal Biotechnology (N Y)
Year 1990
Volume 8
Pages 27-32
Authors Hyde CC, Miles EW
Title The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2190828
Journal Eur J Biochem
Year 1990
Volume 189
Pages 667-73
Authors Sawada S, Akutsu H, Ogasahara K, Yutani K
Title Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1692319
Journal J Biol Chem
Year 1990
Volume 265
Pages 7987-93
Authors Murry-Brelier A, Goldberg ME
Title Mechanism of inactivation of the beta 2 subunit of Escherichia coli tryptophan synthase by monoclonal antibodies.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2053470
Journal Adv Enzymol Relat Areas Mol Biol
Year 1991
Volume 64
Pages 93-172
Authors Miles EW
Title Structural basis for catalysis by tryptophan synthase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1849406
Journal Biochem J
Year 1991
Volume 274
Pages 807-12
Authors Malthouse JP, Milne JJ, Gariani LS
Title A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1868082
Journal Biochemistry
Year 1991
Volume 30
Pages 8067-74
Authors Chaffotte A, Guillou Y, Delepierre M, Hinz HJ, Goldberg ME
Title The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase beta 2-subunit folds into a stable, organized nonnative conformation.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2021608
Journal Biochemistry
Year 1991
Volume 30
Pages 4173-9
Authors Kaufmann M, Schwarz T, Jaenicke R, Schnackerz KD, Meyer HE, Bartholmes P
Title Limited proteolysis of the beta 2-dimer of tryptophan synthase yields an enzymatically active derivative that binds alpha-subunits.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1718750
Journal Eur J Biochem
Year 1991
Volume 201
Pages 681-93
Authors Delepierre M, Larvor MP, Baleux F, Goldberg ME
Title 1H-NMR conformational analysis of a high-affinity antigenic 11-residue peptide from the tryptophan synthase beta 2 subunit.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 1939081
Journal J Biol Chem
Year 1991
Volume 266
Pages 20205-12
Authors Lim WK, Sarkar SK, Hardman JK
Title Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 1346502
Journal Biochemistry
Year 1992
Volume 31
Pages 1180-90
Authors Brzovic PS, Kayastha AM, Miles EW, Dunn MF
Title Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 1567839
Journal Biochemistry
Year 1992
Volume 31
Pages 3831-9
Authors Brzovic PS, Ngo K, Dunn MF
Title Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 1559990
Journal J Biol Chem
Year 1992
Volume 267
Pages 7520-8
Authors Yang XJ, Miles EW
Title Threonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 1309752
Journal J Biol Chem
Year 1992
Volume 267
Pages 526-41
Authors Zhao GP, Somerville RL
Title Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 8268176
Journal Biochemistry
Year 1993
Volume 32
Pages 13981-90
Authors Saab-Rincon G, Froebe CL, Matthews CR
Title Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 8473317
Journal J Biol Chem
Year 1993
Volume 268
Pages 8727-34
Authors Lu Z, Nagata S, McPhie P, Miles EW
Title Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 8325869
Journal J Biol Chem
Year 1993
Volume 268
Pages 14921-31
Authors Zhao GP, Somerville RL
Title A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 8206268
Journal Biochem Soc Trans
Year 1994
Volume 22
Pages 43S
Authors Milne JJ, Malthouse JP
Title A study of the tryptophan synthase catalysed H/D exchange of the alpha-protons of amino acids.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 7929385
Journal J Biol Chem
Year 1994
Volume 269
Pages 26591-3
Authors Schlichting I, Yang XJ, Miles EW, Kim AY, Anderson KS
Title Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthase.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 7487918
Journal Biochem J
Year 1995
Volume 311
Pages 1015-9
Authors Milne JJ, Malthouse JP
Title Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 7626617
Journal Biochemistry
Year 1995
Volume 34
Pages 9466-76
Authors Woehl EU, Dunn MF
Title Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 7615535
Journal J Biol Chem
Year 1995
Volume 270
Pages 17333-8
Authors Ruvinov SB, Ahmed SA, McPhie P, Miles EW
Title Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A).
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8615770
Journal Biochem J
Year 1996
Volume 314
Pages 787-91
Authors Milne JJ, Malthouse JP
Title The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 8674622
Journal Biochem Soc Trans
Year 1996
Volume 24
Pages 133S
Authors Milne JJ, Malthouse JP
Title Enzymatic synthesis of alpha-deuterated amino acids.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8652514
Journal Biochemistry
Year 1996
Volume 35
Pages 7378-86
Authors Hur O, Leja C, Dunn MF
Title Evidence of a low-barrier hydrogen bond in the tryptophan synthase catalytic mechanism.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 8664293
Journal Biochemistry
Year 1996
Volume 35
Pages 5002-13
Authors Pan P, Dunn MF
Title beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex.
Related PDB
Related UniProtKB
[27]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8672457
Journal Biochemistry
Year 1996
Volume 35
Pages 4211-21
Authors Rhee S, Parris KD, Ahmed SA, Miles EW, Davies DR
Title Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.
Related PDB 1ttp 1ttq 1ubs
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 8639683
Journal Biochemistry
Year 1996
Volume 35
Pages 1988-94
Authors Saab-Rincon G, Gualfetti PJ, Matthews CR
Title Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 97352620
PubMed ID 9201907
Journal Biochemistry
Year 1997
Volume 36
Pages 7664-80
Authors Rhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW, Davies DR
Title Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.
Related PDB 2trs 2tsy 2tys
Related UniProtKB P00929 P0A2K1
[30]
Resource
Comments
Medline ID
PubMed ID 9220983
Journal Biochemistry
Year 1997
Volume 36
Pages 8954-61
Authors Rondard P, Bregegere F, Lecroisey A, Delepierre M, Bedouelle H
Title Conformational and functional properties of an undecapeptide epitope fused with the C-terminal end of the maltose binding protein.
Related PDB
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[31]
Resource
Comments
Medline ID
PubMed ID 9220984
Journal Biochemistry
Year 1997
Volume 36
Pages 8962-8
Authors Rondard P, Goldberg ME, Bedouelle H
Title Mutational analysis of an antigenic peptide shows recognition in a loop conformation.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 9020588
Journal Trends Biochem Sci
Year 1997
Volume 22
Pages 22-7
Authors Pan P, Woehl E, Dunn MF
Title Protein architecture, dynamics and allostery in tryptophan synthase channeling.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 10909824
Journal Biochem Soc Trans
Year 1998
Volume 26
Pages S66
Authors Malthouse JP, Fitzpatrick TB, Mahon MM
Title A comparison of some of the methods available for analysing the substrate dependence of the exchange of the alpha-protons of amino acids catalysed by pyridoxal-phosphate-dependent enzymes.
Related PDB
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[34]
Resource
Comments
Medline ID
PubMed ID 9772188
Journal Biochemistry
Year 1998
Volume 37
Pages 14591-604
Authors Jhee KH, McPhie P, Ro HS, Miles EW
Title Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 9692955
Journal Biochemistry
Year 1998
Volume 37
Pages 10653-9
Authors Rhee S, Miles EW, Mozzarelli A, Davies DR
Title Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.
Related PDB
Related UniProtKB
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9548921
Journal Biochemistry
Year 1998
Volume 37
Pages 5394-406
Authors Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I
Title Loop closure and intersubunit communication in tryptophan synthase.
Related PDB 1a50 1a5s 2wsy
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 9700925
Journal Biophys Chem
Year 1998
Volume 73
Pages 265-80
Authors Kishore N, Tewari YB, Akers DL, Goldberg RN, Miles EW
Title A thermodynamic investigation of reactions catalyzed by tryptophan synthase.
Related PDB
Related UniProtKB
[38]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 98204834
PubMed ID 9535826
Journal J Biol Chem
Year 1998
Volume 273
Pages 8553-5
Authors Rhee S, Miles EW, Davies DR
Title Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49.
Related PDB 1a5a 1a5b
Related UniProtKB P00929 P0A2K1
[39]
Resource
Comments
Medline ID
PubMed ID 9837895
Journal J Biol Chem
Year 1998
Volume 273
Pages 33247-53
Authors Schnackerz KD, Mozzarelli A
Title Plasticity of the tryptophan synthase active site probed by 31P NMR spectroscopy.
Related PDB
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[40]
Resource
Comments
Medline ID
PubMed ID 10090734
Journal Biochemistry
Year 1999
Volume 38
Pages 3478-90
Authors Bahar I, Jernigan RL
Title Cooperative fluctuations and subunit communication in tryptophan synthase.
Related PDB
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[41]
Resource
Comments
Medline ID
PubMed ID 10387029
Journal Biochemistry
Year 1999
Volume 38
Pages 7881-90
Authors Fan YX, McPhie P, Miles EW
Title Guanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation.
Related PDB
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[42]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 99435740
PubMed ID 10504236
Journal Biochemistry
Year 1999
Volume 38
Pages 12665-74
Authors Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E
Title Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.
Related PDB 1c29 1c8v 1c9d 1cw2 1cx9
Related UniProtKB P00929 P0A2K1
[43]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10600108
Journal Biochemistry
Year 1999
Volume 38
Pages 16469-80
Authors Weyand M, Schlichting I
Title Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate.
Related PDB 1qop 1qoq
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 10353823
Journal Biochemistry
Year 1999
Volume 38
Pages 7131-41
Authors Woehl E, Dunn MF
Title Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 10353822
Journal Biochemistry
Year 1999
Volume 38
Pages 7118-30
Authors Woehl E, Dunn MF
Title Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 10531312
Journal J Biol Chem
Year 1999
Volume 274
Pages 31189-94
Authors Ro HS, Wilson Miles E
Title Catalytic mechanism of the tryptophan synthase alpha(2)beta(2) complex. Effects of pH, isotopic substitution, and allosteric ligands.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 10329177
Journal J Mol Biol
Year 1999
Volume 288
Pages 753-63
Authors Merz A, Knochel T, Jansonius JN, Kirschner K
Title The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 10507003
Journal Methods Enzymol
Year 1999
Volume 308
Pages 111-45
Authors Anderson KS
Title Fundamental mechanisms of substrate channeling.
Related PDB
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 10386870
Journal Protein Sci
Year 1999
Volume 8
Pages 1200-9
Authors Zitzewitz JA, Gualfetti PJ, Perkons IA, Wasta SA, Matthews CR
Title Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.
Related PDB
Related UniProtKB
[50]
Resource
Comments
Medline ID
PubMed ID 10769125
Journal Biochemistry
Year 2000
Volume 39
Pages 4692-703
Authors Fan YX, McPhie P, Miles EW
Title Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects.
Related PDB
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[51]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
Medline ID 20576265
PubMed ID 11034989
Journal J Biol Chem
Year 2000
Volume 275
Pages 41058-63
Authors Weyand M, Schlichting I
Title Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.
Related PDB 1fuy
Related UniProtKB P00929 P0A2K1
[52]
Resource
Comments
Medline ID
PubMed ID 11412095
Journal Biochemistry
Year 2001
Volume 40
Pages 7421-32
Authors Ferrari D, Yang LH, Miles EW, Dunn MF
Title Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.
Related PDB
Related UniProtKB
[53]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11118452
Journal J Biol Chem
Year 2001
Volume 276
Pages 11062-71
Authors Yamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, Yutani K
Title Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry.
Related PDB 1geq
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 12146962
Journal Biochemistry
Year 2002
Volume 41
Pages 9982-90
Authors Harris RM, Dunn MF
Title Intermediate trapping via a conformational switch in the Na(+)-activated tryptophan synthase bienzyme complex.
Related PDB
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 12146963
Journal Biochemistry
Year 2002
Volume 41
Pages 9991-10001
Authors Hur O, Niks D, Casino P, Dunn MF
Title Proton transfers in the beta-reaction catalyzed by tryptophan synthase.
Related PDB
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[56]
Resource
Comments
Medline ID
PubMed ID 11756459
Journal J Biol Chem
Year 2002
Volume 277
Pages 8194-201
Authors Hettwer S, Sterner R
Title A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.
Related PDB
Related UniProtKB
[57]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11756454
Journal J Biol Chem
Year 2002
Volume 277
Pages 10653-60
Authors Weyand M, Schlichting I, Herde P, Marabotti A, Mozzarelli A
Title Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.
Related PDB 1beu 1k8y 1k8z
Related UniProtKB
[58]
Resource
Comments
Medline ID
PubMed ID 11756456
Journal J Biol Chem
Year 2002
Volume 277
Pages 10647-52
Authors Weyand M, Schlichting I, Marabotti A, Mozzarelli A
Title Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase.
Related PDB 1k3u 1k7e 1k7f
Related UniProtKB
[59]
Resource
Comments
Medline ID
PubMed ID 12460570
Journal J Mol Biol
Year 2002
Volume 324
Pages 677-90
Authors Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I
Title On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.
Related PDB 1k8x 1kfb 1kfc 1kfe 1kfj 1kfk
Related UniProtKB

Comments
This enzyme catalyzes two separate reactions on different chains. The beta chain has got the type II PLP-dependent enzyme fold, whereas the alpha chain has (alpha/beta)8 barrel fold.
The alpha chain catalyzes the conversion of 1-(indol-3-yl)glycerol 3-phosphate (IGP) to indole and glyceraldehyde 3-phosphate (G3P) (Eq.1). Then, the beta chain catalyzes the conversion of serine (Ser) and indole to tryptophan (Trp)(Eq.2).
Although monovalent cation does not interact directly with substrate or intermediate, it promotes some parts of reactions (see [21], [22], [44], [45] & [50]).
Each reaction can be described in terms of RLCP classification as follows:
(Eq.1) IGP = Indole + G3P (or alpha-reaction)
(A) Eliminative double-bond formation (Elimination of indole leads to carbonyl formation)
(Eq.2) Ser + Indole = Trp + H2O (or beta-reaction; beta-replacement among PLP-dependent reactions)
(B) Exchange of double-bonded atoms; Formation of external aldimine (PLP-L-Ser; I00043)
(C) Isomerization (shift of double-bond position) forming a quinonoid intermediate (PLP-Ser; I00182)
(D) Eliminative double-bond formation (Elimination of hydroxyl group from the intermediate) forming an aminoacrylate intermediate (I00171)
(E) Additive double-bond deformation (Addition of indole to the intermediate) forming a quinonoid intermediate (PLP-Trp; I00183)
(F) Isomerization (shift of double-bond position) forming external aldimine
(G) Exchange of double-bonded atoms; Formation of internal aldimine, releasing the product, Trp.
The catalytic reactions proceeds as follows:
(A) Eliminative double-bond formation (Elimination of indole leads to carbonyl formation) (see [29], [38], [42] & [59])
(A1) Thr183 of alpha-chain may act as a modulator for Asp60 by orienting the catalytic residue (see [59]). Asp60 polarize the N-H bond of indole group.
(A2) The first general base, Asp60 of alpha-chain, deprotonates the indole nitrogen, whereas the first general acid protonates the C3 atom of the indole ring (eliminated site of the eliminated group). Here, although the paper [42] suggested that Tyr175 of alpha-chain may play the role as the acid, the other paper [38] reported that Tyr175 is not the essential residue in catalysis, and suggested that Glu49 of alpha-chain may protonate the indole ring. This reaction leads to the tetrahedral transition state at the C3 atom of the indole.
(A3) The second general base, Glu49, deprotonates the C3' hydroxyl group, whilst the second general acid, Asp60, protonates the indole nitrogen atom. This reaction leads to the C3-C3' bond cleavage, and formation of carbonyl group at the C3' atom.
(B) Exchange of double-bonded atoms; Formation of external aldimine (PLP-L-Ser; I00043) (see [17] & [46])
(B1) Asp305 (of beta-chain) may act as a general base to deprotonate the amine group of the incoming substrate, L-serine. The proton must be donated to the sidechain nitrogen of Lys87.
(B2) The activated amine group makes a nucleophilic attack on the C4' atom of PLP, forming a gem-diamine (tetrahedral) intermediate.
(B3) Again, Asp305 may act as a general base to deprotonate the amine group of L-serine, so that the lone pair on the amine group can make a nucleophilic attack on the C4' atom. This reaction leads to the release of Lys87, which is unprotonated for the next reaction.
(C) Isomerization (shift of double-bond position) forming a quinonoid intermediate (PLP-Ser; I00182)
(C1) His86 may modulate the activity of Lys87. (Monovalent ion might affect this reaction (see [45]).
(C2) Lys87 may act as a general base to abstract the alpha-proton of PLP-L-Ser, forming a quinonoid intermediate (PLP-Ser; I00182).
(D) Eliminative double-bond formation (Elimination of hydroxyl group from the intermediate) forming an aminoacrylate intermediate (I00171) (see [46])
(D1) Asp305 acts as a general acid to protonate the hydroxyl group, leading to the elimination of a water molecule and to the double-bond formation between the alpha- and beta-carbon atoms.
(E) Additive double-bond deformation (Addition of indole to the intermediate) forming a quinonoid intermediate (PLP-Trp; I00183) (see [11] & [48])
(E1) Monovalent ion might affect this reaction (see [44]).
(E2) Indole makes a nucleophilic attack on the beta-carbon of the aminoacrylate intermediate (I00171).
(E3) A general base must deprotonate the C-3 proton of the indole group. Glu109 may acts as a general base (see [11]).
(F) Isomerization (shift of double-bond position) forming an external aldimine (PLP-L-Trp; I00181) (see [46]).
(F1) His86 may modulate the activity of Lys87.
(F2) Lys87 may act as a general acid to protonate the alpha-carbon of Trp-PLP, leading to the formation of external aldimine.
(G) Exchange of double-bonded atoms; Formation of internal aldimine, releasing the product, Trp. (This reaction is inverse one of external aldimine formation)
(G1) His86 may act as a general base to deprotonate the amine group of Lys87. The proton must be donated to the leaving nitrogen of L-tryptophan (probably by His86). (As Asp305 is located opposite to Lys87, the nearby His86 may act as a base.)
(G2) The activated amine group of Lys87 makes a nucleophilic attack on the C4' atom of PLP, forming a gem-diamine (tetrahedral) intermediate.
(G3) A general base, probably His86, must deprotonate the amine group of Lys87, so that the lone pair on the amine group can make a nucleophilic attack on the C4' atom. This reaction leads to the release of the product, L-tryptophan.

Created Updated
2004-07-02 2015-07-22