EC number:1.1.1.379

Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.379
Description:(R)-mandelate dehydrogenase.
Alternative Name: D-mandelate dehydrogenase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.379
BRENDA Enzyme Link: BRENDA 1.1.1.379
KEGG Enzyme Link: KEGG1.1.1.379
BioCyc Enzyme Link: BioCyc 1.1.1.379
ExPASy Enzyme Link: ExPASy1.1.1.379
EC2PDB Enzyme Link: EC2PDB 1.1.1.379
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.379
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.379
IntEnz Enzyme Link: IntEnz 1.1.1.379
MEDLINE Enzyme Link: MEDLINE 1.1.1.379

EC number:1.1.1.379

MSA:

1.1.1.379;
Phylogenetic Tree:

1.1.1.379;
Uniprot:
M-CSA:
RHEA:43112 (R)-mandelate + NAD(+) = H(+) + NADH + phenylglyoxylate
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
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References

TitleAuthorsDatePubMed ID
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H2013 Sep 1323954635
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases.Wada Y, Iwai S, Tamura Y, Ando T, Shinoda T, Arai K, Taguchi H2008 Apr18391442
Mechanistic and active-site studies on D(--)-mandelate dehydrogenase from Rhodotorula graminis.Baker DP, Kleanthous C, Keen JN, Weinhold E, Fewson CA1992 Jan 11731758