CATH Classification

Domain Context

CATH Clusters

Superfamily Aldolase class I
Functional Family

Enzyme Information
(S)-2-hydroxy-acid oxidase.
based on mapping to UniProt P05414
(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2).
-!- Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. -!- The rat isoenzyme B also acts as EC -!- Formerly EC
(S)-mandelate dehydrogenase.
based on mapping to UniProt P20932
(S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
-!- While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. -!- Transfers the electron pair from FMNH(2) to a component of the electron transport chain, most probably ubiquinone. -!- It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy. -!- Has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate. -!- It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3- yl)lactate. -!- Esters of mandelate, such as methyl (S)-mandelate, are also substrates.

UniProtKB Entries (2)

Spinacia oleracea
Peroxisomal (S)-2-hydroxy-acid oxidase
Pseudomonas putida
(S)-mandelate dehydrogenase

PDB Structure

External Links
Organism Escherichia
Primary Citation
High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase
Sukumar, N., Dewanti, A.R., Mitra, B., Mathews, F.S.