EC number:1.17.1.8

Enzyme

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     1. Oxidoreductases
        1.17 Acting on CH or CH2 groups
            1.17.1 With NAD+ or NADP+ as acceptor
ID:1.17.1.8
Description:4-hydroxy-tetrahydrodipicolinate reductase.
Alternative Name: Dihydrodipicolinate reductase.
Prosite: PDOC01000;
PDB:
PDBScop
1YL7 8058141; 8058142; 8058141; 8058142; 8058141; 8058142; 8058141; 8058142; 8058141; 8058142; 8058141; 8058142; 8058141; 8058142; 8058141; 8058142;
5UGV 8058141; 8058142; 8058141; 8058142;
1YL6 8058141; 8058142; 8058141; 8058142;
1YL5 8058141; 8058142; 8058141; 8058142;
1P9L 8058141; 8058142; 8058141; 8058142;
 » show all
Cath: 3.30.360.10; 3.40.50.720;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.17.1.8
BRENDA Enzyme Link: BRENDA 1.17.1.8
KEGG Enzyme Link: KEGG1.17.1.8
BioCyc Enzyme Link: BioCyc 1.17.1.8
ExPASy Enzyme Link: ExPASy1.17.1.8
EC2PDB Enzyme Link: EC2PDB 1.17.1.8
ExplorEnz Enzyme Link: ExplorEnz 1.17.1.8
PRIAM enzyme-specific profiles Link: PRIAM 1.17.1.8
IntEnz Enzyme Link: IntEnz 1.17.1.8
MEDLINE Enzyme Link: MEDLINE 1.17.1.8

EC number:1.17.1.8

MSA:

1.17.1.8;
Phylogenetic Tree:

1.17.1.8;
Uniprot:
M-CSA:
RHEA:35331 (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1.[OH2;+0:12]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:12].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1
Reaction
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References

TitleAuthorsDatePubMed ID
NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase.Devenish SR, Blunt JW, Gerrard JA2010 Jun 2420503968
Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics.Pearce FG, Sprissler C, Gerrard JA2008 May18250105
The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity.Cirilli M, Zheng R, Scapin G, Blanchard JS2003 Sep 1612962488
RHEA:35323 (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1.[OH2;+0:12]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:12].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase.Devenish SR, Blunt JW, Gerrard JA2010 Jun 2420503968
Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics.Pearce FG, Sprissler C, Gerrard JA2008 May18250105
The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity.Cirilli M, Zheng R, Scapin G, Blanchard JS2003 Sep 1612962488