EzCatDB: D00094

DB codeD00094
CATH domainDomain 11.10.166.10
Domain 22.160.10.10Catalytic domain
E.C.2.3.1.117
CSA2tdt

CATH domainRelated DB codes (homologues)
2.160.10.10D00464,S00167,D00417

Enzyme Name
Swiss-protKEGG

P56220
Protein name2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
tetrahydropicolinate succinylase
tetrahydrodipicolinate N-succinyltransferase
tetrahydrodipicolinate succinyltransferase
succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase
succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylateN-succinyltransferase
SynonymsEC 2.3.1.117
Tetrahydrodipicolinate N-succinyltransferase
THP succinyltransferase
Tetrahydropicolinate succinylase

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis

Swiss-prot:Accession NumberP56220
Entry nameDAPD_MYCBO
ActivitySuccinyl-CoA + (S)-2,3,4,5-tetrahydropyridine- 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6- oxoheptanedioate.
SubunitHomotrimer.
Subcellular locationCytoplasm.
Cofactor


SubstratesProductsintermediates
KEGG-idC00091C03972C00001C00010C04462
CompoundSuccinyl-CoA2,3,4,5-TetrahydrodipicolinateH2OCoAN-Succinyl-L-2-amino-6-oxoheptanedioate
Typeamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide groupcarboxyl group,imine groupH2Oamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl groupamino acids,amide group,carbohydrate,carboxyl group
1tdtA01UnboundUnbound
UnboundUnboundUnbound
1tdtB01UnboundUnbound
UnboundUnboundUnbound
1tdtC01UnboundUnbound
UnboundUnboundUnbound
2tdtA01UnboundUnbound
UnboundUnboundUnbound
3tdtA01UnboundUnbound
UnboundUnboundUnbound
1tdtA02UnboundUnbound
UnboundUnboundUnbound
1tdtB02UnboundUnbound
UnboundUnboundUnbound
1tdtC02UnboundUnbound
UnboundUnboundUnbound
2tdtA02UnboundUnbound
Bound:COAUnboundIntermediate-analogue:NPI
3tdtA02UnboundUnbound
Bound:COAUnboundBound:26P

Active-site residues
resource
literature [3]
pdbCatalytic residues
1tdtA01
1tdtB01
1tdtC01
2tdtA01
3tdtA01
1tdtA02ASP 141
1tdtB02ASP 141
1tdtC02ASP 141
2tdtA02ASP 141
3tdtA02ASP 141

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.10368-10369
[5]p.975-978

references
[1]
PubMed ID8880935
JournalProteins
Year1996
Volume26
Pages115-7
AuthorsBinder DA, Blanchard JS, Roderick SL
TitleCrystallization and preliminary crystallographic analysis of tetrahydrodipicolinate-N-succinyltransferase.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID97164902
PubMed ID9012664
JournalBiochemistry
Year1997
Volume36
Pages489-94
AuthorsBeaman TW, Binder DA, Blanchard JS, Roderick SL
TitleThree-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB1tdt
Related Swiss-protP56220
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID98337777
PubMed ID9671504
JournalBiochemistry
Year1998
Volume37
Pages10363-9
AuthorsBeaman TW, Blanchard JS, Roderick SL
TitleThe conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase.
Related PDB2tdt,3tdt
Related Swiss-protP56220
[4]
PubMed ID11106178
JournalProtein Sci
Year2000
Volume9
Pages2034-7
AuthorsCirilli M, Scapin G, Sutherland A, Vederas JC, Blanchard JS
TitleThe three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate.
[5]
PubMed ID11910040
JournalProtein Sci
Year2002
Volume11
Pages974-9
AuthorsBeaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL
TitleAcyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.


createdupdated
2004-03-172009-02-26


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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