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1.1.1.379: (R)-mandelate dehydrogenase

This is an abbreviated version!
For detailed information about (R)-mandelate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.379

Reaction

(R)-mandelate
+
NAD+
=
phenylglyoxylate
 +
NADH
 +
H+

Synonyms

D(-)-mandelate dehydrogenase, D-mandelate dehydrogenase, D-ManDH, D-ManDH2, DMDH, LhDMDH, ManDH2, NAD+-dependent D-mandelate dehydrogenase, NAD-dependent D-mandelate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.379 (R)-mandelate dehydrogenase

Inhibitors

Inhibitors on EC 1.1.1.379 - (R)-mandelate dehydrogenase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
(R)-mandelate
substrate inhibition
(S)-Mandelate
competitive
2-hydroxy-2-(4-hydroxyphenyl)propanoate
5 mM, 44.2% inhibition
2-hydroxy-3-methylbutanoate
10 mM, 31.9% inhibition
2-Hydroxy-4-methylpentanoate
1 mM, 55.1% inhibition
2-hydroxyhexanoate
1 mM, 63.8% inhibition
2-hydroxypentanoate
10 mM, 67.4% inhibition
2-oxo-3-methylbutanoate
10 mM, 43.1% inhibition
2-oxo-3-methylpentanoate
5 mM, 54.1% inhibition
2-oxo-4-methylpentanoate
1 mM, 40.4% inhibition
2-oxoglutarate
10 mM, 77.1% inhibition
2-Oxohexanoate
10 mM, 44.1% inhibition
2-oxooctanoate
2.5 mM, 28.5% inhibition
2-oxopentanoate
10 mM, 44.1% inhibition
D-lactate
10 mM, 17.4% inhibition
N-ethylmaleimide
10 mM, strong inhibition
oxalate
10 mM, 63.1% inhibition
oxaloacetate
10 mM, 38.5% inhibition
oxamate
10 mM,% inhibition
phenyl 2-hydroxypropanoate
10 mM, 47.1% inhibition
pyruvate
10 mM, 17.4% inhibition
additional information
neither stimulated nor inhibited by 1 mM concentrations of NaCl, Na2SO4, KCl, MgCl2, NH4Cl, CaCl2, ZnCl2, CoCl2, FeCl3, KH2PO4, NaH2PO4, MnSO4, MnCl2 or CuSO4. Not inhibited by the following metal-chelating agents each at 1 mM: EDTA, diethyldithiocarbamic acid, bathophenanthroline disulfonic acid, dihydroxybenzene disulfonic acid, pyrazole, 8-hydroxyquinoline or 2,2'-dipyridyl. Little or no inhibition of enzyme activity by 10 mM iodoacetate, 10 mM iodoacetamide, 6.65 mM 5,5'-dithiobis(2-nitrobenzoic acid) or 5 mM 4-chloromercuribenzoate, even after a 6 h preincubation at 27°C. Neither inhibited nor stimulated by 1 mM concentrations of benzaldehyde, benzoate, succinate, glucose, ATP/Mg2+, ADP/Mg2+ or acetyl-CoA
-