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Literature summary for 1.2.1.B8 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
Search for more literature for 1.2.1.B8

Cloned(Commentary)

Cloned (Comment) Organism
-
 Levilactobacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0426
-
 5'-hydroxyaverantin pH 7.5, 37°C Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25873
-
 x * 25873, calculated from sequence, TOF MS analysis Levilactobacillus brevis
33000
-
 x * 33000, SDS-PAGE Levilactobacillus brevis
100000
-
 gel filtration Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis
-
-
-
Levilactobacillus brevis IFO 12005
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Levilactobacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.552
-
 pH 7.5, 37°C Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-hydroxyaverantin + NADP+ the enzyme catalyzes a reaction in aflatoxin biosynthesis Levilactobacillus brevis (1'S)-5'-oxoaverantin + NADPH + H+
-
 ?
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+
-
 ?
5'-hydroxyaverantin + NADP+ the enzyme catalyzes a reaction in aflatoxin biosynthesis Levilactobacillus brevis IFO 12005 (1'S)-5'-oxoaverantin + NADPH + H+
-
 ?
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+
-
 ?
additional information no activity with nidurufin, averantin, and 6-phenylhexal-1-ol Levilactobacillus brevis ?
-
 ?
additional information no activity with nidurufin, averantin, and 6-phenylhexal-1-ol Levilactobacillus brevis IFO 12005 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 33000, SDS-PAGE Levilactobacillus brevis
? x * 25873, calculated from sequence, TOF MS analysis Levilactobacillus brevis

Synonyms

Synonyms Comment Organism
Lac-HAVN dehydrogenase
-
 Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Levilactobacillus brevis
40.55
-
-
 Levilactobacillus brevis

Temperature Range [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
 Levilactobacillus brevis
7.5
-
 assay at Levilactobacillus brevis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 pH 6.5: about 75% of maximal activity, pH 8.5: about 30% of maximal activity Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
NADP+ no activity with NAD+ Levilactobacillus brevis