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Literature summary extracted from

  • Ehrensberger, A.H.; Elling, R.A.; Wilson, D.K.
    Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity (2006), Structure, 14, 567-575.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.9
-
Gluconobacter oxydans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.9 hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution Gluconobacter oxydans

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.9 D38S/M39R the mutant enzyme is able to exclusively use NADP+, with no loss of activity Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.9 0.0205
-
NADP+ pH 7.0, mutant enzyme D38S/M39R Gluconobacter oxydans
1.1.1.9 0.348
-
NAD+ pH 7.0, wild-type enzyme Gluconobacter oxydans
1.1.1.9 13.7
-
xylitol pH 7.0, cofactor: NAD+, wild-type enzyme Gluconobacter oxydans
1.1.1.9 100
-
xylitol pH 7.0, cofactor: NADP+ mutant enzyme D38S/M39R Gluconobacter oxydans

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.9 Gluconobacter oxydans Q8GR61
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.9
-
Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.9 xylitol + NAD+
-
Gluconobacter oxydans D-xylulose + NADH + H+
-
?
1.1.1.9 xylitol + NADP+ wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity Gluconobacter oxydans D-xylulose + NADPH + H+
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.9 0.206
-
NADP+ pH 7.0, mutant enzyme D38S/M39R Gluconobacter oxydans
1.1.1.9 17.9
-
xylitol pH 7.0, cofactor: NADP+mutant enzyme D38S/M39R Gluconobacter oxydans
1.1.1.9 24.6
-
xylitol pH 7.0, cofactor: NAD+, wild-type enzyme Gluconobacter oxydans
1.1.1.9 27.2
-
NAD+ pH 7.0, wild-type enzyme Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.9 NAD+ NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose Gluconobacter oxydans
1.1.1.9 NADP+ wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity Gluconobacter oxydans