EC number:4.3.3.7

Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.3 Amine-lyases
ID:4.3.3.7
Description:4-hydroxy-tetrahydrodipicolinate synthase.
Alternative Name: Dihydrodipicolinate synthetase.
DHDPS.
Prosite: PDOC00569;
PDB:
PDBScop
Cath: 3.20.20.70;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.3.7
BRENDA Enzyme Link: BRENDA 4.3.3.7
KEGG Enzyme Link: KEGG4.3.3.7
BioCyc Enzyme Link: BioCyc 4.3.3.7
ExPASy Enzyme Link: ExPASy4.3.3.7
EC2PDB Enzyme Link: EC2PDB 4.3.3.7
ExplorEnz Enzyme Link: ExplorEnz 4.3.3.7
PRIAM enzyme-specific profiles Link: PRIAM 4.3.3.7
IntEnz Enzyme Link: IntEnz 4.3.3.7
MEDLINE Enzyme Link: MEDLINE 4.3.3.7

EC number:4.3.3.7

MSA:

4.3.3.7;
Phylogenetic Tree:

4.3.3.7;
Uniprot:
M-CSA:
RHEA:34171 L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[CH3;+0:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[NH2;+0:7])-[*:8]-[CH;+0:9]=[O;H0;+0:10]>>[*:1]-[CH;+0:2]1-[CH2;+0:3]-[CH;+0:9](-[OH;+0:10])-[*:8]-[C;H0;+0:6](-[*:5])=[N;H0;+0:7]-1.[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R1997 Jan 78993314