DB code: S00243

RLCP classification 4.151.774000.401 : Addition
4.16.66400.7 : Addition
5.41.2776000.400 : Elimination
CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
E.C. 2.5.1.54
CSA
M-CSA
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 S00244 S00199 S00200 S00201 S00221 S00222 S00847 S00224 S00225 S00226 D00014 D00029 M00141 T00015 T00239 D00664 D00665 D00804 D00863 T00089

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AB91 Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive
EC 2.5.1.54
Phospho-2-keto-3-deoxyheptonate aldolase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthetase
NP_415275.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489027.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00793 (DAHP_synth_1)
[Graphical View]
P32449 Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
EC 2.5.1.54
Phospho-2-keto-3-deoxyheptonate aldolase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthetase
NP_009808.1 (Protein)
NM_001178597.1 (DNA/RNA sequence)
PF00793 (DAHP_synth_1)
[Graphical View]

KEGG enzyme name
3-deoxy-7-phosphoheptulonate synthase
2-dehydro-3-deoxy-phosphoheptonate aldolase
2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphatelyase (pyruvate-phosphorylating)
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonateD-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
D-erythrose-4-phosphate-lyase
D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
DAH7-P synthase
DAHP synthase
DS-Co
DS-Mn
KDPH synthase
KDPH synthetase
deoxy-D-arabino-heptulosonate-7-phosphate synthetase
phospho-2-dehydro-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptanoate aldolase
phospho-2-keto-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptonic aldolase
phospho-2-oxo-3-deoxyheptonate aldolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AB91 AROG_ECOLI Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate. Homotetramer.
P32449 AROG_YEAST Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

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

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00034 C00074 C00279 C00001 C04691 C00009
E.C.
Compound Manganese Phosphoenolpyruvate D-Erythrose 4-phosphate H2O 2-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate Orthophosphate Transition-state with an oxocarbenium ion A linear tetrahedral intermediate
Type heavy metal carboxyl group,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion H2O carbohydrate,carboxyl group,phosphate group/phosphate ion phosphate group/phosphate ion
ChEBI 18291
 35154
 18291
 35154
 		44897
 44897
 		48153
 48153
 		15377
 15377
 		18150
 18150
 		26078
 26078
PubChem 23930
 23930
 		1005
 58114173
 59658623
 1005
 58114173
 59658623
 		122357
 122357
 		22247451
 962
 22247451
 962
 		160647
 160647
 		1004
 22486802
 1004
 22486802
1gg1A Bound:_MN Analogue:PGA Unbound Unbound Analogue:SO4_1373 Unbound Unbound
1gg1B Bound:_MN Analogue:PGA Unbound Unbound Analogue:SO4_2373 Unbound Unbound
1gg1C Bound:_MN Analogue:PGA Unbound Unbound Analogue:SO4_3373 Unbound Unbound
1gg1D Bound:_MN Analogue:PGA Unbound Unbound Analogue:SO4_4373 Unbound Unbound
1qr7A Analogue:_PB Bound:PEP Unbound Unbound Analogue:SO4 Unbound Unbound
1qr7B Analogue:_PB Bound:PEP Unbound Unbound Analogue:SO4 Unbound Unbound
1qr7C Analogue:_PB Bound:PEP Unbound Unbound Analogue:SO4 Unbound Unbound
1qr7D Analogue:_PB Bound:PEP Unbound Unbound Analogue:SO4 Unbound Unbound
1kflA Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflB Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflC Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflD Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflE Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflF Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflG Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1kflH Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1n8fA Bound:_MN Bound:PEP Unbound Unbound Analogue:SO4_5353 Unbound Unbound
1n8fB Bound:_MN Bound:PEP Unbound Unbound Analogue:SO4_2353 Unbound Unbound
1n8fC Bound:_MN Bound:PEP Unbound Unbound Analogue:SO4_3353 Unbound Unbound
1n8fD Bound:_MN Bound:PEP Unbound Unbound Analogue:SO4_4353 Unbound Unbound
1hfbA Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbB Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbC Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbD Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbE Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbF Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbG Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1hfbH Unbound Bound:PEP Unbound Unbound Unbound Unbound Unbound
1oabA Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1oabB Bound:_MN Bound:PEP Unbound Unbound Unbound Unbound Unbound
1of8A Analogue:_CO Bound:PEP Analogue:G3P Bound:HOH_2003 Unbound Unbound Unbound Unbound
1of8B Analogue:_CO Bound:PEP Analogue:G3P Bound:HOH_2003 Unbound Unbound Unbound Unbound
1ofaA Analogue:_CO Bound:PEP Unbound Unbound Unbound Unbound Unbound
1ofaB Analogue:_CO Bound:PEP Unbound Unbound Unbound Unbound Unbound
1ofpA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ofpB Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ofpC Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ofpD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ofqA Bound:_MN Unbound Unbound Unbound Unbound Unbound Unbound
1ofqB Bound:_MN Unbound Unbound Unbound Unbound Unbound Unbound
1ofqC Bound:_MN Unbound Unbound Unbound Unbound Unbound Unbound
1ofqD Bound:_MN Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature[8] & [15]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1gg1A LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1gg1B LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1gg1C LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1gg1D LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1qr7A LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1qr7B LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1qr7C LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1qr7D LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflA LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflB LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflC LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflD LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflE LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflF LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflG LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1kflH LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1n8fA LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1n8fB LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1n8fC LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1n8fD LYS 97;GLU 143;LYS 186;ARG 165;ARG 234 CYS 61;HIS 268;GLU 302;ASP 326(Manganese binding) ALA 164
1hfbA LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbB LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbC LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbD LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbE LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbF LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbG LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1hfbH LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1oabA LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1oabB LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1of8A LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1of8B LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1ofaA LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1ofaB LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76;HIS 282;GLU 316;ASP 342(Manganese binding) ALA 179
1ofpA ; ;LYS 201;ARG 180;ARG 249 CYS 76; ;GLU 316;ASP 342(Manganese binding) ALA 179 invisible 111-120, 281-288
1ofpB LYS 112;GLU 158;LYS 201;ARG 180;ARG 249 CYS 76; ;GLU 316;ASP 342(Manganese binding) ALA 179 invisible 281-288
1ofpC ; ;LYS 201;ARG 180;ARG 249 CYS 76; ;GLU 316;ASP 342(Manganese binding) ALA 179 invisible 111-120, 281-288
1ofpD ; ;LYS 201;ARG 180;ARG 249 CYS 76; ;GLU 316;ASP 342(Manganese binding) ALA 179 invisible 111-120, 281-288
1ofqA LYS 1112;GLU 1158;LYS 1201;ARG 1180;ARG 1249 CYS 1076;HIS 1282;GLU 1316;ASP 1342(Manganese binding) ALA 1179 invisible 1114-1116
1ofqB ; ;LYS 2201;ARG 2180;ARG 2249 CYS 2076;HIS 2282;GLU 2316;ASP 2342(Manganese binding) ALA 2179 invisilbe 2112/2117-2118/2158
1ofqC LYS 3112;GLU 3158;LYS 3201;ARG 3180;ARG 3249 CYS 3076;HIS 3282;GLU 3316;ASP 3342(Manganese binding) ALA 3179 invisible 3115-3116
1ofqD ; ;LYS 4201;ARG 4180;ARG 4249 CYS 4076;HIS 4282;GLU 4316;ASP 4342(Manganese binding) ALA 4179 invisilbe 4112/2158

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.1, p.4615-4616
[4]
p.871-872
[5]
Fig.1, Fig.5, p.394-395 3
[8]
[12]
[13]
p.3775
[15]
p.687

References
[1]
Resource
Comments
Medline ID
PubMed ID 8643451
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 4612-6
Authors Li Y, Evans JN
Title The hard-soft acid-base principle in enzymatic catalysis: dual reactivity of phosphoenolpyruvate.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8778789
Journal Proteins
Year 1996
Volume 24
Pages 404-6
Authors Shumilin IA, Kretsinger RH, Bauerle R
Title Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9398312
Journal Biochemistry
Year 1997
Volume 36
Pages 15817-22
Authors Akowski JP, Bauerle R
Title Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID 99354419
PubMed ID 10425687
Journal Structure Fold Des
Year 1999
Volume 7
Pages 865-75
Authors Shumilin IA, Kretsinger RH, Bauerle RH
Title Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.
Related PDB 1qr7
Related UniProtKB P0AB91
[5]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10926516
Journal J Mol Biol
Year 2000
Volume 301
Pages 389-99
Authors Wagner T, Shumilin IA, Bauerle R, Kretsinger RH
Title Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis.
Related PDB 1gg1
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10987918
Journal J Org Chem
Year 2000
Volume 65
Pages 5891-7
Authors Sundaram AK, Woodard RW
Title Probing the stereochemistry of E. coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-sensitive)-catalyzed synthesis of KDO 8-P analogues.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11444986
Journal Biochemistry
Year 2001
Volume 40
Pages 8387-96
Authors Jordan PA, Bohle DS, Ramilo CA, Evans JN
Title New insights into the metal center of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11732901
Journal Biochemistry
Year 2001
Volume 40
Pages 14821-8
Authors Parker EJ, Bulloch EM, Jameson GB, Abell C
Title Substrate deactivation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by erythrose 4-phosphate.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11381336
Journal Curr Microbiol
Year 2001
Volume 42
Pages 426-31
Authors Lin LL, Liao HF, Chien HR, Hsu WH
Title Identification of essential cysteine residues in 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Corynebacterium glutamicum.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11476485
Journal Nat Prod Rep
Year 2001
Volume 18
Pages 334-55
Authors Knaggs AR
Title The biosynthesis of shikimate metabolites.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11429861
Journal Org Lett
Year 2001
Volume 3
Pages 21-4
Authors Sundaram AK, Woodard RW
Title Neisseria gonorrhoeae 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase does not catalyze the formation of the ribo analogue.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 12126632
Journal J Mol Biol
Year 2002
Volume 320
Pages 1147-56
Authors Shumilin IA, Zhao C, Bauerle R, Kretsinger RH
Title Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates.
Related PDB 1kfl
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12667068
Journal Biochemistry
Year 2003
Volume 42
Pages 3766-76
Authors Shumilin IA, Bauerle R, Kretsinger RH
Title The high-resolution structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase reveals a twist in the plane of bound phosphoenolpyruvate.
Related PDB 1n8f
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12540830
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 862-7
Authors Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH
Title Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 15019786
Journal J Mol Biol
Year 2004
Volume 337
Pages 675-90
Authors Konig V, Pfeil A, Braus GH, Schneider TR
Title Substrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism.
Related PDB 1hfb 1ofp 1ofq 1ofa 1of8
Related UniProtKB

Comments
Formerly EC 4.1.2.15, transferred to 2.5.1.54.
This enzyme catalyze three successive reactions, two additive reactions and an elimination.
According to the literature [15], two possible mechanisms have been proposed so far. The earlier studies proposed a reaction mechanism, in which the metal-activated water initiates the reaction (see [5], [13] & [15]). However, considering the stereochemistry, it is unlikely. Instead, the literature [15] proposed an alternative mechanism.
According to the alternative mechanism, this enzyme catalyzes the following three reactions successively.
(A) Addition of the double-bonded carbon of PEP to the carbonyl group of another substrate, E4P, leading to the formation of oxocarbenium ion and hydroxyl oxygen from carbonyl oxygen:
(A1) The pi-electrons on the C3=C2 double-bond of PEP make a nucleophilic attack from the si-face onto the re-face of the metal-activated aldehyde group of E4P, to form a covalent bond.
(A2) Lys112 acts as a general acid, which protonates the C1-carbonyl oxygen of E4P, converting the carbonyl oxygen to hydroxyl one.
(B) Addition of water to the oxocarbenium-ion intermediate, created by the condensation of PEP and E4P:
(B1) Glu158 acts as a general base, activating a water molecule positioned on the re-side (opposite to si-face) of PEP. Here, Lys112 act as a second general base, accepting the proton of Glu158, left over by the attacking water.
(B2) The activated water, the hydroxide ion, makes a nucleophilic attack on the oxocarbenium ion (C2 atom of originarily PEP), leading to the a linear intermediate.
(C) Elimination of phosphate oxygen leading to formation of carbonyl group (cf. [2] & S00243):
(C1) Sidechains of Arg180 and Arg249, and mainchain amide of Ala179 stabilize the negative charge on the eliminated phosphate group.
(C2) Lys201 acts as a general acid, which donates a proton to the eliminated phosphate group, leading to the cleavage of the C-O bond.
(C3) Lys201 acts as a general base to deprotonate the hydroxyl group (created by the attacking water), leading to the formation of the carbonyl group.
During these reactions, metal ions, such as manganese, assisted the reactions by interacting with the substrates.

Created Updated
2004-04-04 2009-02-26