EzCatDB: D00028

DB codeD00028
CATH domainDomain 13.40.50.720Catalytic domain
Domain 23.30.360.10Catalytic domain
E.C.1.3.1.26
CSA1arz

CATH domainRelated DB codes (homologues)
3.30.360.10T00219,D00003,D00010,D00017,D00023,D00027,D00034,D00476
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
Swiss-protKEGG

P04036
Protein nameDihydrodipicolinate reductasedihydrodipicolinate reductase
dihydrodipicolinic acid reductase
2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase
SynonymsDHPR
EC 1.3.1.26

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis

Swiss-prot:Accession NumberP04036
Entry nameDAPB_ECOLI
Activity2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H.
SubunitHomotetramer.
Subcellular locationCytoplasm.
Cofactor


SubstratesProducts
KEGG-idC03972C00006C00003C03340C00004C00005C00080
Compound2,3,4,5-TetrahydrodipicolinateNADP+NAD+2,3-DihydrodipicolinateNADHNADPHH+
Typecarboxyl group,imine groupamide group,amine group,nucleotideamide group,amine group,nucleotidearomatic ring (with nitrogen atoms),carboxyl groupamide group,amine group,nucleotideamide group,amine group,nucleotideothers
1arzA01UnboundUnboundUnboundUnboundUnboundUnbound
1arzB01UnboundUnboundBound:NADUnboundUnboundUnbound
1arzC01UnboundUnboundBound:NADUnboundUnboundUnbound
1arzD01UnboundUnboundBound:NADUnboundUnboundUnbound
1dihA01UnboundUnboundUnboundUnboundUnboundBound:NDP
1druA01UnboundUnboundUnboundUnboundBound:NADUnbound
1drvA01UnboundUnboundAnalogue:A3DUnboundUnboundUnbound
1drwA01UnboundUnboundAnalogue:NHDUnboundUnboundUnbound
1arzA02UnboundUnboundUnboundUnboundUnboundUnbound
1arzB02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound
1arzC02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound
1arzD02UnboundUnboundUnboundAnalogue:PDCUnboundUnbound
1dihA02UnboundUnboundUnboundUnboundUnboundUnbound
1druA02UnboundUnboundUnboundUnboundUnboundUnbound
1drvA02UnboundUnboundUnboundUnboundUnboundUnbound
1drwA02UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [4]
pdbCatalytic residues
1arzA01
1arzB01
1arzC01
1arzD01
1dihA01
1druA01
1drvA01
1drwA01
1arzA02HIS 159;LYS 163
1arzB02HIS 159;LYS 163
1arzC02HIS 159;LYS 163
1arzD02HIS 159;LYS 163
1dihA02HIS 159;LYS 163
1druA02HIS 159;LYS 163
1drvA02HIS 159;LYS 163
1drwA02HIS 159;LYS 163

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Scheme 3, p.3499-3500
[4]Fig.4, p.15087-15088

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID95200850
PubMed ID7893645
JournalBiochemistry
Year1995
Volume34
Pages3502-12
AuthorsScapin G, Blanchard JS, Sacchettini JC
TitleThree-dimensional structure of Escherichia coli dihydrodipicolinate reductase.
Related Swiss-protP04036
[2]
CommentsX-ray crystallography
PubMed ID7893644
JournalBiochemistry
Year1995
Volume34
Pages3492-501
AuthorsReddy SG, Sacchettini JC, Blanchard JS
TitleExpression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase.
Related PDB1dih
[3]
PubMed ID8873595
JournalBiochemistry
Year1996
Volume35
Pages13294-302
AuthorsReddy SG, Scapin G, Blanchard JS
TitleInteraction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
Related PDB1drw,1drv,1dru
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID98060760
PubMed ID9398235
JournalBiochemistry
Year1997
Volume36
Pages15081-8
AuthorsScapin G, Reddy SG, Zheng R, Blanchard JS
TitleThree-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
Related PDB1arz
Related Swiss-protP04036
[5]
PubMed ID11342032
JournalBiochim Biophys Acta
Year2001
Volume1545
Pages67-77
AuthorsPaiva AM, Vanderwall DE, Blanchard JS, Kozarich JW, Williamson JM, Kelly TM
TitleInhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis.


createdupdated
2004-03-242009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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