Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.108
Description:Carnitine 3-dehydrogenase.

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.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.108
BRENDA Enzyme Link: BRENDA 1.1.1.108
KEGG Enzyme Link: KEGG1.1.1.108
BioCyc Enzyme Link: BioCyc 1.1.1.108
ExPASy Enzyme Link: ExPASy1.1.1.108
EC2PDB Enzyme Link: EC2PDB 1.1.1.108
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.108
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.108
IntEnz Enzyme Link: IntEnz 1.1.1.108
MEDLINE Enzyme Link: MEDLINE 1.1.1.108
MSA:

1.1.1.108;

Phylogenetic Tree:

1.1.1.108;

Uniprot:
M-CSA:
RHEA:19265 carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
[Kinetic studies of the reaction mechanism of carnitine dehydrogenase of Pseudomonas aeruginosa].Schöpp W, Sorger H, Kleber HP, Aurich H1969 Aug4310279
[Purification and properties of carnitine dehydrogenase from Pseudomonas aeruginosa].Aurich H, Kleber HP, Sorger H, Tauchert H1968 Nov4302217