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Literature summary for 1.1.1.379 extracted from

  • Baker, D.P.; Kleanthous, C.; Keen, J.N.; Weinhold, E.; Fewson, C.A.
    Mechanistic and active-site studies on D(-)-mandelate dehydrogenase from Rhodotorula graminis (1992), Biochem. J., 281 (Pt 1), 211-218.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(2R)-[(bromoacetyl)oxy]mandelic acid 8 mM, greater than 95% inactivation after 2 h at 27°C. Inactivation is a pseudo-first-order process. D-Mandelate protects against inactivation. The inhibitor is covalently bound Rhodotorula graminis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-mandelate + NAD+ Rhodotorula graminis first enzyme of the mandelate pathway in the yeast Rhodotorula graminis phenylglyoxylate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Rhodotorula graminis Q7LLW9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mandelate + NAD+ first enzyme of the mandelate pathway in the yeast Rhodotorula graminis Rhodotorula graminis phenylglyoxylate + NADH + H+
-
?
(R)-mandelate + NAD+ the enzyme transfers the pro-R hydrogen atom from NADH during the reduction of phenylglyoxylate Rhodotorula graminis phenylglyoxylate + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
D(-)-mandelate dehydrogenase
-
Rhodotorula graminis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.9
-
assay at Rhodotorula graminis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4
-
(2R)-[(bromoacetyl)oxy]mandelic acid pH 5.9, temperature not specified in the publication Rhodotorula graminis