Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chen, L.; Bai, Y.; Fan, T.P.; Zheng, X.; Cai, Y.
    Characterization of a D-lactate dehydrogenase from Lactobacillus fermentum JN248 with high phenylpyruvate reductive activity (2017), J. Food Sci., 82, 2269-2275 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.28 expression in Escherichia coli Limosilactobacillus fermentum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.28 1.2
-
NADH pH 8, 50°C Limosilactobacillus fermentum
1.1.1.28 1.68
-
phenylpyruvate pH 8, 50°C Limosilactobacillus fermentum

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.28 Limosilactobacillus fermentum
-
-
-
1.1.1.28 Limosilactobacillus fermentum JN248
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.28 2-oxobutanoate + NADH + H+ 12.6% of the activity with pyruvate Limosilactobacillus fermentum (R)-2-hydroxybutanoate + NAD+
-
?
1.1.1.28 2-oxobutanoate + NADH + H+ 12.6% of the activity with pyruvate Limosilactobacillus fermentum JN248 (R)-2-hydroxybutanoate + NAD+
-
?
1.1.1.28 3,4-dihydroxyphenylpyruvate + NADH + H+ 43.1% of the activity with pyruvate Limosilactobacillus fermentum (R)-3,4-dihydroxyphenyllactate + NAD+
-
?
1.1.1.28 3,4-dihydroxyphenylpyruvate + NADH + H+ 43.1% of the activity with pyruvate Limosilactobacillus fermentum JN248 (R)-3,4-dihydroxyphenyllactate + NAD+
-
?
1.1.1.28 3-methyl-2-oxobutanoate + NADH + H+ 19.4% of the activity with pyruvate Limosilactobacillus fermentum (R)-2-hydroxy-3-methylbutanoate + NAD+
-
?
1.1.1.28 additional information enzyme displays more than 99% enantioselectivity. No substrates: 3-methyl-2-oxopentanoate, 4-methyl-2-oxopentanoate, indole-3-pyruvate Limosilactobacillus fermentum ?
-
-
1.1.1.28 additional information enzyme displays more than 99% enantioselectivity. No substrates: 3-methyl-2-oxopentanoate, 4-methyl-2-oxopentanoate, indole-3-pyruvate Limosilactobacillus fermentum JN248 ?
-
-
1.1.1.28 phenylpyruvate + NADH + H+ 70.4% of the activity with pyruvate Limosilactobacillus fermentum (R)-3-phenyllactate + NAD+
-
?
1.1.1.28 phenylpyruvate + NADH + H+ 70.4% of the activity with pyruvate Limosilactobacillus fermentum JN248 (R)-3-phenyllactate + NAD+
-
?
1.1.1.28 pyruvate + NADH + H+
-
Limosilactobacillus fermentum (R)-lactate + NAD+
-
?
1.1.1.28 pyruvate + NADH + H+
-
Limosilactobacillus fermentum JN248 (R)-lactate + NAD+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.28 ? x * 43000, SDS-PAGE Limosilactobacillus fermentum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.28 D-LDH0653
-
Limosilactobacillus fermentum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.28 50
-
-
Limosilactobacillus fermentum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.28 67.4
-
NADH pH 8, 50°C Limosilactobacillus fermentum
1.1.1.28 122.7
-
phenylpyruvate pH 8, 50°C Limosilactobacillus fermentum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.28 8
-
-
Limosilactobacillus fermentum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.28 7 9 more than 90% of maximum activity Limosilactobacillus fermentum
1.1.1.28 10
-
70% residual activity Limosilactobacillus fermentum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.28 56.16
-
NADH pH 8, 50°C Limosilactobacillus fermentum
1.1.1.28 73.01
-
phenylpyruvate pH 8, 50°C Limosilactobacillus fermentum