Enzyme

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     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.1 With NAD+ or NADP+ as acceptor
ID:1.2.1.90
Description:Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)).
Alternative Name: Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase.
GAPN.
Cath: 3.40.605.10; 3.40.309.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.1.90
BRENDA Enzyme Link: BRENDA 1.2.1.90
KEGG Enzyme Link: KEGG1.2.1.90
BioCyc Enzyme Link: BioCyc 1.2.1.90
ExPASy Enzyme Link: ExPASy1.2.1.90
EC2PDB Enzyme Link: EC2PDB 1.2.1.90
ExplorEnz Enzyme Link: ExplorEnz 1.2.1.90
PRIAM enzyme-specific profiles Link: PRIAM 1.2.1.90
IntEnz Enzyme Link: IntEnz 1.2.1.90
MEDLINE Enzyme Link: MEDLINE 1.2.1.90
MSA:

1.2.1.90;

Phylogenetic Tree:

1.2.1.90;

Uniprot:
M-CSA:
RHEA:42760 D-glyceraldehyde 3-phosphate + H2O + NAD(+) = 3-phospho-D-glycerate + 2 H(+) + NADH
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[CH;+0:10]-[*:11].[OH2;+0:12]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.Brunner NA, Brinkmann H, Siebers B, Hensel R1998 Mar 139497334
Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax.Hensel R, Laumann S, Lang J, Heumann H, Lottspeich F1987 Dec 303121324
The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation.Ahmed H, Ettema TJ, Tjaden B, Geerling AC, van der Oost J, Siebers B2005 Sep 115869466
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.Pohl E, Brunner N, Wilmanns M, Hensel R2002 May 3111842090
Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level.Brunner NA, Siebers B, Hensel R2001 Apr11354453

RHEA:14669 D-glyceraldehyde 3-phosphate + H2O + NADP(+) = 3-phospho-D-glycerate + 2 H(+) + NADPH
RULE(radius=1) [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[CH;+0:10]-[*:11].[OH2;+0:12]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.Brunner NA, Brinkmann H, Siebers B, Hensel R1998 Mar 139497334
Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax.Hensel R, Laumann S, Lang J, Heumann H, Lottspeich F1987 Dec 303121324
The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation.Ahmed H, Ettema TJ, Tjaden B, Geerling AC, van der Oost J, Siebers B2005 Sep 115869466
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E2004 Aug 1315288789
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.Pohl E, Brunner N, Wilmanns M, Hensel R2002 May 3111842090