EC number:1.2.1.16

Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.1 With NAD+ or NADP+ as acceptor
ID:1.2.1.16
Description:Succinate-semialdehyde dehydrogenase (NAD(P)(+)).
Prosite: PDOC00068;
PDB:
PDBScop
Cath: 3.40.605.10; 3.40.309.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.1.16
BRENDA Enzyme Link: BRENDA 1.2.1.16
KEGG Enzyme Link: KEGG1.2.1.16
BioCyc Enzyme Link: BioCyc 1.2.1.16
ExPASy Enzyme Link: ExPASy1.2.1.16
EC2PDB Enzyme Link: EC2PDB 1.2.1.16
ExplorEnz Enzyme Link: ExplorEnz 1.2.1.16
PRIAM enzyme-specific profiles Link: PRIAM 1.2.1.16
IntEnz Enzyme Link: IntEnz 1.2.1.16
MEDLINE Enzyme Link: MEDLINE 1.2.1.16

EC number:1.2.1.16

MSA:

1.2.1.16;
Phylogenetic Tree:

1.2.1.16;
Uniprot:
M-CSA:
RHEA:13217 H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH + succinate
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
Kinetic studies with rat-brain succinic-semialdehyde dehydrogenase.Rivett AJ, Tipton KF1981 Jun7262085
Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida.Sànchez M, Alvarez MA, Balaña R, Garrido-Pertierra A1988 Apr 143355840
Purification and properties of rat brain succinic semialdehyde dehydrogenase.Cash C, Ciesielski L, Maitre M, Mandel P197719091
Computational prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in Escherichia coli.Fuhrer T, Chen L, Sauer U, Vitkup D2007 Nov17873044
A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism.Watanabe S, Kodaki T, Makino K2006 Sep 2916835232
Final steps in the catabolism of nicotine.Chiribau CB, Mihasan M, Ganas P, Igloi GL, Artenie V, Brandsch R2006 Apr16689938
Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides.Busch KB, Fromm H1999 Oct10517851
Elucidation of the trigonelline degradation pathway reveals previously undescribed enzymes and metabolites.Perchat N, Saaidi PL, Darii E, Pellé C, Petit JL, Besnard-Gonnet M, de Berardinis V, Dupont M, Gimbernat A, Salanoubat M, Fischer C, Perret A2018 May 829686076
RHEA:13213 H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH + succinate
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
Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD).Bartsch K, von Johnn-Marteville A, Schulz A1990 Dec2254272
Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases.Jaeger M, Rothacker B, Ilg T2008 Aug 118474219
Computational prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in Escherichia coli.Fuhrer T, Chen L, Sauer U, Vitkup D2007 Nov17873044
Final steps in the catabolism of nicotine.Chiribau CB, Mihasan M, Ganas P, Igloi GL, Artenie V, Brandsch R2006 Apr16689938