EzCatDB: S00197

DB codeS00197
CATH domainDomain 13.20.20.60Catalytic domain
E.C.4.1.2.20
CSA1dxe

CATH domainRelated DB codes (homologues)
3.20.20.60S00241,T00217,S00242,T00043,D00477

Enzyme Name
Swiss-protKEGG

P23522
Protein name5-keto-4-deoxy-D-glucarate aldolase2-dehydro-3-deoxyglucarate aldolase
2-keto-3-deoxyglucarate aldolase
alpha-keto-beta-deoxy-D-glucarate aldolase
2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase
SynonymsKDGluc aldolase
KDGlucA
EC 4.1.2.20
5-dehydro-4-deoxy-D-glucarate aldolase
2-keto-3-deoxy-D-glucarate aldolase
2-dehydro-3-deoxy-D-glucarate aldolase
Alpha-keto-beta-deoxy-D-glucarate aldolase

KEGG pathways
MAP codePathways
MAP00053Ascorbate and aldarate metabolism

Swiss-prot:Accession NumberP23522
Entry nameGARL_ECOLI
Activity5-dehydro-4-deoxy-D-glucarate = pyruvate + tartronate semialdehyde.,2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde.
SubunitHomohexamer, trimer of dimers.
Subcellular location
CofactorBinds 1 magnesium ion per subunit. Can also use, although less efficiently, Co(2+), Fe(2+) and Mn(2+).


CofactorsSubstratesProducts
KEGG-idC00305C03921C00022C01146
CompoundMagnesium2-Dehydro-3-deoxy-D-glucaratePyruvateTartronate semialdehyde
Typedivalent metal (Ca2+, Mg2+)carbohydrate,carboxyl groupcarbohydrate,carboxyl groupcarbohydrate,carboxyl group
1dxeABound:_MGUnboundUnboundUnbound
1dxeBBound:_MGUnboundUnboundUnbound
1dxfABound:_MGUnboundBound:PYRUnbound
1dxfBBound:_MGUnboundBound:PYRUnbound

Active-site residues
resource
literature [3]
pdbCatalytic residuesCofactor-binding residues
1dxeAHIS 50;ARG 75
GLU 153;ASP 179(Magnesium binding)
1dxeBHIS 50;ARG 75
GLU 153;ASP 179(Magnesium binding)
1dxfAHIS 50;ARG 75
GLU 153;ASP 179(Magnesium binding)
1dxfBHIS 50;ARG 75
GLU 153;ASP 179(Magnesium binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.3851-3852

references
[1]
PubMed ID10393309
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages1368-9
AuthorsBlackwell NC, Cullis PM, Cooper RA, Izard T
TitleRhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli.
[2]
PubMed ID11053844
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages1437-9
AuthorsHendry EJ, Buchanan CL, Russell RJ, Hough DW, Reeve CD, Danson MJ, Taylor GL
TitlePreliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID20380920
PubMed ID10921867
JournalEMBO J
Year2000
Volume19
Pages3849-56
AuthorsIzard T, Blackwell NC
TitleCrystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.
Related PDB1dxe,1dxf
Related Swiss-protP23522


createdupdated
2004-03-302009-03-19


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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