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Literature summary extracted from

  • Wada, Y.; Iwai, S.; Tamura, Y.; Ando, T.; Shinoda, T.; Arai, K.; Taguchi, H.
    A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases (2008), Biosci. Biotechnol. Biochem., 72, 1087-1094.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.345 expression in Escherichia coli Enterococcus faecalis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.345 0.13
-
4-methyl-2-oxopentanoate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 0.18
-
3-methyl-2-oxobutanoate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 0.25
-
phenylglyoxylate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 0.3
-
2-oxopentanoate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 0.9
-
(R)-mandelate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 1.5
-
2-Oxohexanoate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 5.7
-
2-oxo-3-phenylpropanoate pH 7.5, 30°C Enterococcus faecalis
1.1.1.345 9.5
-
2-oxobutanoate pH 7.5, 30°C Enterococcus faecalis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.345 34331
-
x * 34331, calculated from nucleotide sequence Enterococcus faecalis
1.1.1.345 40000
-
x * 40000, SDS-PAGE Enterococcus faecalis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.345 Enterococcus faecalis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.345 (R)-mandelate + NAD+ Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis phenylglyoxylate + NADH + H+
-
?
1.1.1.345 2-oxo-3-phenylpropanoate + NADH + H+ Vmax/KM is 1.9% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis 2-hydroxy-3-phenylpropanoate + NAD+
-
?
1.1.1.345 2-oxobutanoate + NADH + H+ Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis 2-hydroxybutanoate + NAD+
-
?
1.1.1.345 2-oxohexanoate + NADH + H+ Vmax/KM is 3% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis 2-hydroxyhexanoate + NAD+
-
?
1.1.1.345 2-oxopentanoate + NADH + H+ Vmax/KM is 10.6% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis 2-hydroxypentanoate + NAD+
-
?
1.1.1.345 3-methyl-2-oxobutanoate + NADH + H+ Vmax/KM is 56% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis 3-methyl-2-hydroxybutanoate + NAD+
-
?
1.1.1.345 4-methyl-2-oxopentanoate + NADH + H+ highest Vmax/Km value of all substrates tested Enterococcus faecalis 4-methyl-2-hydroxypentanoate + NAD+
-
?
1.1.1.345 additional information the recombinant enzyme exhibits high catalytic activity toward various 2-oxoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-oxoisovalerate Enterococcus faecalis ?
-
?
1.1.1.345 phenylglyoxylate + NADH + H+ Vmax/KM is 54% compared to 4-methyl-2-oxopentanoate Enterococcus faecalis hydroxy(phenyl)acetic acid + NAD+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.345 ? x * 40000, SDS-PAGE Enterococcus faecalis
1.1.1.345 ? x * 34331, calculated from nucleotide sequence Enterococcus faecalis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.345 D-mandelate dehydrogenase misleading Enterococcus faecalis
1.1.1.345 D-ManDH2
-
Enterococcus faecalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.345 30
-
assay at Enterococcus faecalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.345 7.5
-
assay at Enterococcus faecalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.345 NAD+ strict coenzyme specificity for NADH and NAD+ Enterococcus faecalis
1.1.1.345 NADH strict coenzyme specificity for NADH and NAD+ Enterococcus faecalis