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Literature summary extracted from

  • Sakuno, E.; Kameyama, M.; Nakajima, H.; Yabe, K.
    Purification and gene cloning of a dehydrogenase from Lactobacillus brevis that catalyzes a reaction involved in aflatoxin biosynthesis (2008), Biosci. Biotechnol. Biochem., 72, 724-734.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.352
-
Levilactobacillus brevis
1.2.1.B8
-
Levilactobacillus brevis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.352 0.0426
-
5'-hydroxyaverantin in 30 mM potassium phosphate buffer (pH 7.5), at 37°C Levilactobacillus brevis
1.2.1.B8 0.0426
-
5'-hydroxyaverantin pH 7.5, 37°C Levilactobacillus brevis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.352 25873
-
3 * 25873, calculated from amino acid sequence Levilactobacillus brevis
1.1.1.352 25918
-
3 * 25918 MALDI TOF mass spectrometry Levilactobacillus brevis
1.1.1.352 33000
-
3 * 33000, SDS-PAGE Levilactobacillus brevis
1.1.1.352 100000
-
gel filtration Levilactobacillus brevis
1.2.1.B8 25873
-
x * 25873, calculated from sequence, TOF MS analysis Levilactobacillus brevis
1.2.1.B8 33000
-
x * 33000, SDS-PAGE Levilactobacillus brevis
1.2.1.B8 100000
-
gel filtration Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.352 5'-hydroxyaverantin + NADP+ Levilactobacillus brevis
-
5'-oxoaverantin + NADPH + H+
-
ir
1.1.1.352 5'-hydroxyaverantin + NADP+ Levilactobacillus brevis IFO 12005
-
5'-oxoaverantin + NADPH + H+
-
ir
1.2.1.B8 5'-hydroxyaverantin + NADP+ Levilactobacillus brevis the enzyme catalyzes a reaction in aflatoxin biosynthesis (1'S)-5'-oxoaverantin + NADPH + H+
-
?
1.2.1.B8 5'-hydroxyaverantin + NADP+ Levilactobacillus brevis IFO 12005 the enzyme catalyzes a reaction in aflatoxin biosynthesis (1'S)-5'-oxoaverantin + NADPH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.352 Levilactobacillus brevis
-
-
-
1.1.1.352 Levilactobacillus brevis IFO 12005
-
-
-
1.2.1.B8 Levilactobacillus brevis
-
-
-
1.2.1.B8 Levilactobacillus brevis IFO 12005
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.352 DEAE Sepharose CL-6B column chromatography, phenyl Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration Levilactobacillus brevis
1.2.1.B8
-
Levilactobacillus brevis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.352 0.00613
-
cell extract, at pH 7.5 and 37°C Levilactobacillus brevis
1.1.1.352 0.552
-
after 90fold purification, at pH 7.5 and 37°C Levilactobacillus brevis
1.2.1.B8 0.552
-
pH 7.5, 37°C Levilactobacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.352 5'-hydroxyaverantin + NADP+
-
Levilactobacillus brevis 5'-oxoaverantin + NADPH + H+
-
ir
1.1.1.352 5'-hydroxyaverantin + NADP+
-
Levilactobacillus brevis IFO 12005 5'-oxoaverantin + NADPH + H+
-
ir
1.1.1.352 additional information no activity with NAD+ Levilactobacillus brevis ?
-
?
1.1.1.352 additional information no activity with NAD+ Levilactobacillus brevis IFO 12005 ?
-
?
1.2.1.B8 5'-hydroxyaverantin + NADP+ the enzyme catalyzes a reaction in aflatoxin biosynthesis Levilactobacillus brevis (1'S)-5'-oxoaverantin + NADPH + H+
-
?
1.2.1.B8 5'-hydroxyaverantin + NADP+ a mixture of two diastereomers, (1'S,5'R)-hydroxyaverantin and (1'S,5'S)-hydroxyaverantin Levilactobacillus brevis (1'S)-5'-oxoaverantin + NADPH + H+
-
?
1.2.1.B8 5'-hydroxyaverantin + NADP+ the enzyme catalyzes a reaction in aflatoxin biosynthesis Levilactobacillus brevis IFO 12005 (1'S)-5'-oxoaverantin + NADPH + H+
-
?
1.2.1.B8 5'-hydroxyaverantin + NADP+ a mixture of two diastereomers, (1'S,5'R)-hydroxyaverantin and (1'S,5'S)-hydroxyaverantin Levilactobacillus brevis IFO 12005 (1'S)-5'-oxoaverantin + NADPH + H+
-
?
1.2.1.B8 additional information no activity with nidurufin, averantin, and 6-phenylhexal-1-ol Levilactobacillus brevis ?
-
?
1.2.1.B8 additional information no activity with nidurufin, averantin, and 6-phenylhexal-1-ol Levilactobacillus brevis IFO 12005 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.352 homotrimer 3 * 33000, SDS-PAGE Levilactobacillus brevis
1.1.1.352 homotrimer 3 * 25873, calculated from amino acid sequence Levilactobacillus brevis
1.1.1.352 homotrimer 3 * 25918 MALDI TOF mass spectrometry Levilactobacillus brevis
1.2.1.B8 ? x * 33000, SDS-PAGE Levilactobacillus brevis
1.2.1.B8 ? x * 25873, calculated from sequence, TOF MS analysis Levilactobacillus brevis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.352 alcohol dehydrogenase
-
Levilactobacillus brevis
1.1.1.352 HAVN dehydrogenase
-
Levilactobacillus brevis
1.2.1.B8 Lac-HAVN dehydrogenase
-
Levilactobacillus brevis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.352 40 55
-
Levilactobacillus brevis
1.2.1.B8 37
-
assay at Levilactobacillus brevis
1.2.1.B8 40.55
-
-
Levilactobacillus brevis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.1.B8 35 60 35°C: about 65% of maximal activity, 60°C: about 30% of maximal activity Levilactobacillus brevis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.352 7 8 no activity is detected above pH 9.0 Levilactobacillus brevis
1.2.1.B8 7 8
-
Levilactobacillus brevis
1.2.1.B8 7.5
-
assay at Levilactobacillus brevis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.B8 6.5 8.5 pH 6.5: about 75% of maximal activity, pH 8.5: about 30% of maximal activity Levilactobacillus brevis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.352 NADP+ no activity with NAD+ Levilactobacillus brevis
1.2.1.B8 NADP+ no activity with NAD+ Levilactobacillus brevis