Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.7
Description:Saccharopine dehydrogenase (NAD(+), L-lysine-forming).
Alternative Name: Lysine-2-oxoglutarate reductase.
Cath: 3.30.360.10; 3.40.50.720;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.7
BRENDA Enzyme Link: BRENDA 1.5.1.7
KEGG Enzyme Link: KEGG1.5.1.7
BioCyc Enzyme Link: BioCyc 1.5.1.7
ExPASy Enzyme Link: ExPASy1.5.1.7
EC2PDB Enzyme Link: EC2PDB 1.5.1.7
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.7
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.7
IntEnz Enzyme Link: IntEnz 1.5.1.7
MEDLINE Enzyme Link: MEDLINE 1.5.1.7
MSA:

1.5.1.7;

Phylogenetic Tree:

1.5.1.7;

Uniprot:
M-CSA:
RHEA:12440 H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH;+0:4]-[*:5].[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1.[OH2;+0:14]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:14].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1.[*:5]-[NH2;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Active-site residues of saccharopine dehydrogenase (NAD+, lysine-forming) from baker's yeast.Fujioka M1981 Aug7021257
Chemical mechanism of saccharopine dehydrogenase (NAD+, L-lysine-forming) as deduced from initial rate pH studies.Fujioka M1984 May 16712252
A kinetic study of saccharopine dehydrogenase reaction.Fujioka M, Nakatani Y1970 Sep4318475
Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase.Saunders PP, Broquist HP1966 Jul 254287986
A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae.Xu H, Alguindigue SS, West AH, Cook PF2007 Jan 2317223709
Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae.Xu H, West AH, Cook PF2006 Oct 317002315