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

BRENDA support

Literature summary extracted from

  • Watanabe, S.; Kodaki, T.; Kodak, T.; Makino, K.
    Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism (2006), J. Biol. Chem., 281, 2612-2623.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.376 overexpression in Escherichia coli Azospirillum brasilense

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.376 D168A mutant shows no activity under standard assay conditions Azospirillum brasilense
1.1.1.376 N172A kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme Azospirillum brasilense

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.376 0.109
-
D-galactose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 0.255
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 0.26
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 0.785
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 1.41
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 1.49
-
D-galactose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 2 10 D-xylose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 3.95
-
D-talose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 5.87
-
D-talose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 28.9
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 42.5
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 72
-
D-xylose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.376 additional information no significant increase in activity in the presence of MgCl2, MnCl2, ZnCl2, CoCl2, NiCl2, or CaCl2 at final concentrations of 1 mM Azospirillum brasilense

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.376 33664
-
1 * 33664, calculated from sequence Azospirillum brasilense
1.1.1.376 39500
-
1 * 39500, SDS-PAGE Azospirillum brasilense
1.1.1.376 46400
-
gel filtration Azospirillum brasilense

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.376 L-arabinose + NADP+ Azospirillum brasilense first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose L-arabinono-1,4-lactone + NADPH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.376 Azospirillum brasilense Q53TZ2
-
-
1.1.1.376 Azospirillum brasilense DSM 1690 Q53TZ2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.376
-
Azospirillum brasilense

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.376 0.042
-
pH 9.0, 30°C, L-arabinose + NAD+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 0.148
-
pH 9.0, 30°C, L-arabinose + NADP+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 1.7
-
pH 9.0, 30°C, D-talose + NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 5.3
-
pH 9.0, 30°C, D-xylose + NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 12.8
-
pH 9.0, 30°C, D-talose + NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 14.8
-
pH 9.0, 30°C, D-xylose + NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 14.9
-
pH 9.0, 30°C, L-arabinose + NAD+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 23.8
-
pH 9.0, 30°C, D-galactose + NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 25
-
pH 9.0, 30°C, L-arabinose + NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 32
-
pH 9.0, 30°C, L-arabinose + NADP+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 35.6
-
pH 9.0, 30°C, D-galactose + NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 44.9
-
pH 9.0, 30°C, L-arabinose + NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.376 D-galactose + NAD+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense ?
-
?
1.1.1.376 D-galactose + NAD+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense DSM 1690 ?
-
?
1.1.1.376 D-galactose + NADP+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense ?
-
?
1.1.1.376 D-galactose + NADP+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense DSM 1690 ?
-
?
1.1.1.376 D-talose + NAD+ low activity Azospirillum brasilense ?
-
?
1.1.1.376 D-talose + NADP+ low activity Azospirillum brasilense ?
-
?
1.1.1.376 D-xylose + NAD+ low activity Azospirillum brasilense ?
-
?
1.1.1.376 D-xylose + NAD+ low activity Azospirillum brasilense DSM 1690 ?
-
?
1.1.1.376 D-xylose + NADP+ low activity Azospirillum brasilense ?
-
?
1.1.1.376 D-xylose + NADP+ low activity Azospirillum brasilense DSM 1690 ?
-
?
1.1.1.376 L-arabinose + NAD+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense L-arabinono-1,4-lactone + NADH + H+
-
?
1.1.1.376 L-arabinose + NADP+ first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose Azospirillum brasilense L-arabinono-1,4-lactone + NADPH + H+
-
?
1.1.1.376 L-arabinose + NADP+ the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+ Azospirillum brasilense L-arabinono-1,4-lactone + NADPH + H+
-
?
1.1.1.376 additional information no activity with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose (less than 1% of the activity with L-arabinose) Azospirillum brasilense ?
-
?
1.1.1.376 additional information no activity with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose (less than 1% of the activity with L-arabinose) Azospirillum brasilense DSM 1690 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.376 monomer 1 * 39500, SDS-PAGE Azospirillum brasilense
1.1.1.376 monomer 1 * 33664, calculated from sequence Azospirillum brasilense

Synonyms

EC Number Synonyms Comment Organism
1.1.1.376 L-arabinose 1-dehydrogenase ambiguous Azospirillum brasilense

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.376 30
-
assay at Azospirillum brasilense

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.376 0.1
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 0.3
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 1.04
-
D-talose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 4
-
D-xylose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 6.1
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 9.7
-
D-talose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 12
-
D-xylose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 16.5
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 19
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 19.8
-
D-galactose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 26
-
D-galactose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 33.3
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.376 9
-
assay at Azospirillum brasilense

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.376 NAD+ the enzyme prefers NADP+ over NAD+ Azospirillum brasilense
1.1.1.376 NADP+ the enzyme prefers NADP+ over NAD+ Azospirillum brasilense

Expression

EC Number Organism Comment Expression
1.1.1.376 Azospirillum brasilense the gene is induced by L-arabinose but not by D-galactose up

General Information

EC Number General Information Comment Organism
1.1.1.376 malfunction a disruptant of the L-arabinose 1-dehydrogenase gene does not grow on L-arabinose but grows on D-galactose at the same growth rate as the wild-type strain Azospirillum brasilense

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.376 0.01
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 0.019
-
D-xylose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 0.03
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A Azospirillum brasilense
1.1.1.376 0.17
-
D-xylose pH 9.0, 30°C, cofactor: NADP*, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 0.26
-
D-talose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 1.6
-
D-talose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 7.78
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 13.3
-
D-galactose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 13.4
-
L-arabinose pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 63.5
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme Azospirillum brasilense
1.1.1.376 131
-
L-arabinose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense
1.1.1.376 240
-
D-galactose pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense Azospirillum brasilense