Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.99 With unknown physiological acceptors
ID:1.1.99.31
Description:(S)-mandelate dehydrogenase.
Alternative Name: MDH.
L(+)-mandelate dehydrogenase.
Prosite: PDOC00482;
PDB:
PDBScop
Cath: 3.20.20.70;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.99.31
BRENDA Enzyme Link: BRENDA 1.1.99.31
KEGG Enzyme Link: KEGG1.1.99.31
BioCyc Enzyme Link: BioCyc 1.1.99.31
ExPASy Enzyme Link: ExPASy1.1.99.31
EC2PDB Enzyme Link: EC2PDB 1.1.99.31
ExplorEnz Enzyme Link: ExplorEnz 1.1.99.31
PRIAM enzyme-specific profiles Link: PRIAM 1.1.99.31
IntEnz Enzyme Link: IntEnz 1.1.99.31
MEDLINE Enzyme Link: MEDLINE 1.1.99.31
MSA:

1.1.99.31;

Phylogenetic Tree:

1.1.99.31;

Uniprot:
M-CSA:
RHEA:15749 (S)-mandelate + A = AH2 + phenylglyoxylate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain.Illias RM, Sinclair R, Robertson D, Neu A, Chapman SK, Reid GA1998 Jul 19639569
Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity.Dewanti AR, Xu Y, Mitra B2004 Aug 2415311930
Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism.Dewanti AR, Xu Y, Mitra B2004 Feb 2414967029
High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase.Sukumar N, Dewanti AR, Mitra B, Mathews FS2004 Jan 3014604988
Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase.Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS2001 Aug 2111502180
(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.Lehoux IE, Mitra B1999 May 410231535