×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Aldolase class I
Functional Family

Enzyme Information

1.1.3.15
(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 1.4.3.2. -!- Formerly EC 1.1.3.1.
1.1.99.31
(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)

P05414
GOX_SPIOL
Spinacia oleracea
Peroxisomal (S)-2-hydroxy-acid oxidase
P20932
MDLB_PSEPU
Pseudomonas putida
(S)-mandelate dehydrogenase

PDB Structure

PDB 1HUV
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase.
Sukumar, N., Xu, Y., Gatti, D.L., Mitra, B., Mathews, F.S.
Biochemistry
CATH-Gene3D is a Global Biodata Core Resource Learn more...