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

BRENDA support

Literature summary for 1.1.1.122 extracted from

  • Ohshiro, T.; Morita, N.
    Production and characterization of L-fucose dehydrogenase from newly isolated Acinetobacter sp. strain SA-134 (2014), Prep. Biochem. Biotechnol., 44, 382-391.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ag+ complete inhibition at 1 mM Acinetobacter sp.
Co2+ complete inhibition at 1 mM Acinetobacter sp.
Cu2+ complete inhibition at 1 mM Acinetobacter sp.
EDTA
-
Acinetobacter sp.
Hg2+ complete inhibition at 1 mM Acinetobacter sp.
N-ethylmaleimide
-
Acinetobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7
-
NADP+ at pH 8.0 and 37°C Acinetobacter sp.
2.6
-
L-fucose at pH 8.0 and 37°C Acinetobacter sp.
2.7
-
NAD+ at pH 8.0 and 37°C Acinetobacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
gel filtration Acinetobacter sp.
25000
-
1 * 25000, SDS-PAGE Acinetobacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-fucose + NADP+ Acinetobacter sp. 100% activity L-fuconolactone + NADPH + H+
-
?
L-fucose + NADP+ Acinetobacter sp. SA-134 100% activity L-fuconolactone + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
-
-
Acinetobacter sp. SA-134
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose column chromatography, phenyl-Toyopearl column chromatography, Q-Sepharose column chromatography, Superdex 200HR gel filtration, and Mono Q column chromatography Acinetobacter sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3
-
cell-free extract, at pH 8.0 and 37°C Acinetobacter sp.
217
-
after 94.3fold purification, at pH 8.0 and 37°C Acinetobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-arabinose + NADP+ good substrate with 65% activity compared to L-fucose Acinetobacter sp. D-arabinolactone + NADPH + H+
-
?
D-arabinose + NADP+ good substrate with 65% activity compared to L-fucose Acinetobacter sp. SA-134 D-arabinolactone + NADPH + H+
-
?
L-fucose + NAD+
-
Acinetobacter sp. L-fuconolactone + NADH + H+
-
?
L-fucose + NAD+
-
Acinetobacter sp. SA-134 L-fuconolactone + NADH + H+
-
?
L-fucose + NADP+ good substrate Acinetobacter sp. L-fuconolactone + NADPH + H+
-
?
L-fucose + NADP+ 100% activity Acinetobacter sp. L-fuconolactone + NADPH + H+
-
?
L-fucose + NADP+ good substrate Acinetobacter sp. SA-134 L-fuconolactone + NADPH + H+
-
?
L-fucose + NADP+ 100% activity Acinetobacter sp. SA-134 L-fuconolactone + NADPH + H+
-
?
L-galactose + NADP+ L-galactose is a poor substrate with 11% activity compared to L-fucose Acinetobacter sp. ?
-
?
additional information no activity with D-glucose, D-fructose, D-galactose, L-arabinose, D-mannose, L-rhamnose, D-xylose, maltose, sucrose, and lactose Acinetobacter sp. ?
-
?
additional information no activity with D-glucose, D-fructose, D-galactose, L-arabinose, D-mannose, L-rhamnose, D-xylose, maltose, sucrose, and lactose Acinetobacter sp. SA-134 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 25000, SDS-PAGE Acinetobacter sp.

Synonyms

Synonyms Comment Organism
L-fucose dehydrogenase
-
Acinetobacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Acinetobacter sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
the enzyme is stable below 35°C for 60 min Acinetobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Acinetobacter sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 the enzyme is stable between pH 6.0 and 10.0 for 60 min Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme acts on both NAD+ and NADP+ in similar manner Acinetobacter sp.
NADP+ the enzyme acts on both NAD+ and NADP+ in similar manner Acinetobacter sp.