EzCatDB: D00476

DB codeD00476
CATH domainDomain 13.40.50.720
Domain 23.30.360.10Catalytic domain
E.C.1.2.1.59
CSA1cf2

CATH domainRelated DB codes (homologues)
3.30.360.10T00219,D00003,D00010,D00017,D00023,D00027,D00028,D00034
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,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,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

P10618P39460
Protein nameGlyceraldehyde-3-phosphate dehydrogenaseGlyceraldehyde-3-phosphate dehydrogenaseglyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)(phosphorylating)
triosephosphate dehydrogenase (NAD(P))
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
SynonymsGAPDH
EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
GAPDH
EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00710Carbon fixation in photosynthetic organisms

Swiss-prot:Accession NumberP10618P39460
Entry nameG3P_METFEG3P_SULSO
ActivityD-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
SubunitHomotetramer.Homotetramer.
Subcellular locationCytoplasm.Cytoplasm.
Cofactor



SubstratesProducts
KEGG-idC00118C00009C00003C00006C00236C00004C00005C00080
CompoundD-Glyceraldehyde 3-phosphateOrthophosphateNAD+NADP+3-Phospho-D-glyceroyl phosphateNADHNADPHH+
Typecarbohydrate,phosphate group/phosphate ionphosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotideothers
1b7gO01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b7gQ01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cf2O01UnboundUnboundUnboundBound:NAPUnboundUnboundUnbound
1cf2P01UnboundUnboundUnboundBound:NAPUnboundUnboundUnbound
1cf2Q01UnboundUnboundUnboundBound:NAPUnboundUnboundUnbound
1cf2R01UnboundUnboundUnboundBound:NAPUnboundUnboundUnbound
1b7gO02UnboundAnalogue:SO4 601UnboundUnboundUnboundUnboundUnbound
1b7gQ02UnboundAnalogue:SO4 602UnboundUnboundUnboundUnboundUnbound
1cf2O02UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnbound
1cf2P02UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnbound
1cf2Q02UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnbound
1cf2R02UnboundAnalogue:SO4UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1b7g & literature [5], [6] & [9]
pdbCatalytic residuescomment
1b7gO01
mutant I2V
1b7gQ01
mutant I2V
1cf2O01

1cf2P01

1cf2Q01

1cf2R01

1b7gO02CYS 139;HIS 219

1b7gQ02CYS 139;HIS 219

1cf2O02CYS 140;HIS 219

1cf2P02CYS 140;HIS 219

1cf2Q02CYS 140;HIS 219

1cf2R02CYS 140;HIS 219


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.655-656
[6]p.495-497
[9]p.115-117

references
[1]
PubMed ID9761871
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages671-4
AuthorsFleming TM, Jones CE, Piper PW, Cowan DA, Isupov MN, Littlechild JA
TitleCharacterization, crystallization and preliminary X-ray investigation of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
[2]
PubMed ID9632884
JournalBiochemistry (Mosc)
Year1998
Volume63
Pages504-15
AuthorsNagradova NK, Schmalhausen EV
TitleD-Glyceraldehyde-3-phosphate dehydrogenase: structural basis and functional role of the acyl transfer reactions.
[3]
CommentsX-ray crystallography
PubMed ID10393306
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages1353-5
AuthorsCharron C, Talfournier F, Isupov MN, Branlant G, Littlechild JA, Vitoux B, Aubry A
TitleCrystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus.
Related PDB1cf2
[4]
PubMed ID10491162
JournalEur J Biochem
Year1999
Volume265
Pages93-104
AuthorsTalfournier F, Colloc'h N, Mornon JP, Branlant G
TitleFunctional characterization of the phosphorylating D-glyceraldehyde 3-phosphate dehydrogenase from the archaeon Methanothermus fervidus by comparative molecular modelling and site-directed mutagenesis.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS)
Medline ID99380409
PubMed ID10448043
JournalJ Mol Biol
Year1999
Volume291
Pages651-60
AuthorsIsupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA
TitleCrystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
Related PDB1b7g
Related Swiss-protP39460
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID20181873
PubMed ID10715215
JournalJ Mol Biol
Year2000
Volume297
Pages481-500
AuthorsCharron C, Talfournier F, Isupov MN, Littlechild JA, Branlant G, Vitoux B, Aubry A
TitleThe crystal structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution.
Related Swiss-protP10618
[7]
PubMed ID12369901
JournalCurr Protein Pept Sci
Year2001
Volume2
Pages61-72
AuthorsBrune B, Mohr S
TitleProtein thiol modification of glyceraldehyde-3-phosphate dehydrogenase and caspase-3 by nitric oxide.
[8]
PubMed ID11438534
JournalJ Biol Chem
Year2001
Volume276
Pages35247-52
AuthorsQi J, Isupov MN, Littlechild JA, Anderson LE
TitleChloroplast glyceraldehyde-3-phosphate dehydrogenase contains a single disulfide bond located in the C-terminal extension to the B subunit.
[9]
PubMed ID11265453
JournalMethods Enzymol
Year2001
Volume331
Pages105-17
AuthorsLittlechild JA, Isupov M
TitleGlyceraldehyde-3-phosphate dehydrogenase from Sulfolobus solfataricus.
[10]
PubMed ID12382287
JournalBiopolymers
Year2002
Volume65
Pages263-73
AuthorsCharron C, Vitoux B, Aubry A
TitleComparative analysis of thermoadaptation within the archaeal glyceraldehyde-3-phosphate dehydrogenases from mesophilic Methanobacterium bryantii and thermophilic Methanothermus fervidus.
[11]
PubMed ID11742130
JournalProtein Sci
Year2002
Volume11
Pages137-46
AuthorsOrru S, Ruoppolo M, Francese S, Vitagliano L, Marino G, Esposito C
TitleIdentification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase.
[12]
PubMed ID15046583
JournalBiochem Soc Trans
Year2004
Volume32
Pages255-8
AuthorsLittlechild JA, Guy JE, Isupov MN
TitleHyperthermophilic dehydrogenase enzymes.
[13]
PubMed ID15048777
JournalBiopolymers
Year2004
Volume73
Pages533-41
AuthorsWaingeh VF, Lowe SL, Thomasson KA
TitleBrownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin.

comments
There are several types of glyceraldehyde-3-phosphate dehydrogenases:
NADP-dependent GAPDH (E.C. 1.2.1.9)
NAD(P)-dependent GAPDH (phosphorylating) (E.C. 1.2.1.59)
GAPDH (phosphorylating) (E.C. 1.2.1.12)
NADP-dependent GAPDH (phosphorylating) (E.C. 1.2.1.13)
This enzyme corresponds to NAD(P)-dependent GAPDH (phosphorylating) (E.C. 1.2.1.59).

createdupdated
2005-01-142009-02-26


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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.