Information on EC 1.1.1.379 - (R)-mandelate dehydrogenase

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The expected taxonomic range for this enzyme is: Rhodotorula graminis

EC NUMBER
COMMENTARY hide
1.1.1.379
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RECOMMENDED NAME
GeneOntology No.
(R)-mandelate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(R)-mandelate:NAD+ 2-oxidoreductase
The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
show the reaction diagram
Q7LLW9
first enzyme of the mandelate pathway in the yeast Rhodotorula graminis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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no activity with NADP+, 2,6-dichloroindophenol or 2,6-dichloroindophenol plus N-methylphenazonium methosulfate as electron acceptors
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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neither stimulated nor inhibited by 1 mM concentrations of NaCl, Na2SO4, KCl, MgCl2, NH4Cl, CaCl2, ZnCl2, CoCl2, FeCl3, KH2PO4, NaH2PO4, MnSO4, MnCl2, or CuSO4
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-[(bromoacetyl)oxy]mandelic acid
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8 mM, greater than 95% inactivation after 2 h at 27C. Inactivation is a pseudo-first-order process. D-Mandelate protects against inactivation. The inhibitor is covalently bound
(S)-Mandelate
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competitive
2-hydroxy-2-(4-hydroxyphenyl)propanoate
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5 mM, 44.2% inhibition
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2-hydroxy-3-methylbutanoate
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10 mM, 31.9% inhibition
2-Hydroxy-4-methylpentanoate
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1 mM, 55.1% inhibition
2-hydroxyhexanoate
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1 mM, 63.8% inhibition
2-hydroxypentanoate
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10 mM, 67.4% inhibition
2-oxo-3-methylbutanoate
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10 mM, 43.1% inhibition
2-oxo-3-methylpentanoate
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5 mM, 54.1% inhibition
2-oxo-4-methylpentanoate
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1 mM, 40.4% inhibition
2-oxoglutarate
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10 mM, 77.1% inhibition
2-Oxohexanoate
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10 mM, 44.1% inhibition
2-oxooctanoate
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2.5 mM, 28.5% inhibition
2-Oxopentanoate
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10 mM, 44.1% inhibition
D-lactate
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10 mM, 17.4% inhibition
N-ethylmaleimide
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10 mM, strong inhibition
oxalate
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10 mM, 63.1% inhibition
oxaloacetate
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10 mM, 38.5% inhibition
Oxamate
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10 mM,% inhibition
phenyl 2-hydroxypropanoate
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10 mM, 47.1% inhibition
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pyruvate
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10 mM, 17.4% inhibition
additional information
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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 27C. Neither inhibited nor stimulated by 1 mM concentrations of benzaldehyde, benzoate, succinate, glucose, ATP/Mg2+, ADP/Mg2+ or acetyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.325 - 3.05
(R)-mandelate
0.0775 - 0.309
NAD+
0.026 - 0.038
NADH
0.0455 - 0.0707
phenylglyoxylate
additional information
additional information
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at all pH values tested, the apparent Km-values for NADH and phenylglyoxylate are significantly lower than for NAD+ and (R)-mandelate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
(2R)-[(bromoacetyl)oxy]mandelic acid
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pH 5.9, temperature not specified in the publication
8.2
(S)-Mandelate
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pH 9.5, 27C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67.6
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pH 9.5, 27C, substrate: (R)-mandelate, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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oxidation of R-mandelate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme is crystallized in three different forms using the hanging drop vapour diffusion method at 15-20C. Type I crystals belong to space group P222(1), P22(1)2(1) or P2(1)2(1)2(1) with a = 100.3 A, b = 117.4 A, c = 80.4 A and are likely to contain a dimer in the crystallographic asymmetric unit
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE