DB code: S00201

CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
E.C. 4.2.1.52
CSA 1dhp
M-CSA 1dhp
MACiE M0267

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 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
P0A6L2 4-hydroxy-tetrahydrodipicolinate synthase
HTPA synthase
EC 4.3.3.7
NP_416973.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490706.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00701 (DHDPS)
[Graphical View]

KEGG enzyme name
dihydrodipicolinate synthase
dihydropicolinate synthetase
dihydrodipicolinic acid synthase
L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate andcyclizing)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A6L2 DAPA_ECOLI L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H(2)O. Homotetramer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00300 Lysine biosynthesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00238 C00441 C00022 C03340 C00001
E.C.
Compound Potassium L-Aspartate 4-semialdehyde Pyruvate 2,3-Dihydrodipicolinate H2O
Type univalent metal (Na+, K+) amino acids,carbohydrate carbohydrate,carboxyl group aromatic ring (with nitrogen atoms),carboxyl group H2O
ChEBI 29103
 29103
 		18051
 537519
 18051
 537519
 		32816
 32816
 		18042
 18042
 		15377
 15377
PubChem 813
 813
 		439235
 5287708
 439235
 5287708
 		1060
 1060
 		439982
 439982
 		22247451
 962
 22247451
 962
1dhpA Bound:__K Unbound Unbound Unbound
1dhpB Bound:__K Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1dhp & Swiss-prot;P0A6L2

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dhpA LYS 161;TYR 133
1dhpB LYS 161;TYR 133

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.1, p.231 6
[3]
Fig.7, p.30-32 5
[4]
Scheme 5, p.1739 8
[5]
Fig.1 5
[6]
Fig.1 3

References
[1]
Resource
Comments
Medline ID
PubMed ID 1463470
Journal Biochem J
Year 1992
Volume 288
Pages 691-5
Authors Laber B, Gomis-Ruth FX, Romao MJ, Huber R
Title Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 95156485
PubMed ID 7853400
Journal J Mol Biol
Year 1995
Volume 246
Pages 227-39
Authors Mirwaldt C, Korndorfer I, Huber R
Title The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.
Related PDB 1dhp
Related UniProtKB P0A6L2
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY, AND CATALYTIC MECHANISM.
Medline ID 97146458
PubMed ID 8993314
Journal Biochemistry
Year 1997
Volume 36
Pages 24-33
Authors Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R
Title Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.
Related PDB
Related UniProtKB P0A6L2
[4]
Resource
Comments
Medline ID
PubMed ID 9048556
Journal Biochemistry
Year 1997
Volume 36
Pages 1730-9
Authors Karsten WE
Title Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9417939
Journal J Mol Biol
Year 1997
Volume 274
Pages 608-21
Authors Blickling S, Beisel HG, Bozic D, Knablein J, Laber B, Huber R
Title Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9047371
Journal J Mol Biol
Year 1997
Volume 266
Pages 381-99
Authors Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM
Title Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12711733
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 5694-9
Authors Joerger AC, Mayer S, Fersht AR
Title Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-06-28 2009-03-19