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Literature summary for 1.1.1.14 extracted from

  • Wulf, H.; Mallin, H.; Bornscheuer, U.
    Protein engineering of a thermostable polyol dehydrogenase (2012), Enzyme Microb. Technol., 51, 217-224.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Deinococcus geothermalis

Protein Variants

Protein Variants Comment Organism
D55N mutation located at the NAD+ binding cleft, changes cofactor specificity frm NADH to NADPH Deinococcus geothermalis
additional information substitution of the substrate-binding loop by the loop-region of the galactitol dehydrogenase from Rhodobacter sphaeroides (PDH-158). The substrate scope of this chimera basically represents the average of both wild-type enzymes, with an increase in thermal stability. The amino acid positions Q157 and N161 in the PDH-loop variant seem to have an essential role, variants containing mutations at these sites exhibit decreased enzyme activities. Variants containing mutations V97A or N99L do not lead to a significant activity loss Deinococcus geothermalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
0.15
-
NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
0.41
-
NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
0.44
-
NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Organism

Organism UniProt Comment Textmining
Deinococcus geothermalis Q1J2J0
-
-
Deinococcus geothermalis DSM 11300 Q1J2J0
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
936
-
substrate D-sorbitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1013
-
substrate 1,2-butanediol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1427
-
substrate D-galactitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
2742
-
substrate 1,2-hexanediol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
4659
-
substrate D-xylitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-butanediol + NAD+
-
Deinococcus geothermalis ? + NADH + H+
-
?
1,2-butanediol + NAD+
-
Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
?
1,2-hexanediol + NAD+
-
Deinococcus geothermalis ? + NADH + H+
-
?
1,2-hexanediol + NAD+
-
Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
?
D-galactitol + NAD+
-
Deinococcus geothermalis D-tagatose + NADH + H+
-
?
D-galactitol + NAD+
-
Deinococcus geothermalis DSM 11300 D-tagatose + NADH + H+
-
?
D-sorbitol + NAD+
-
Deinococcus geothermalis L-sorbose + NADH + H+
-
?
D-sorbitol + NAD+
-
Deinococcus geothermalis DSM 11300 L-sorbose + NADH + H+
-
?
D-xylitol + NAD+
-
Deinococcus geothermalis ? + NADH + H+
-
?
D-xylitol + NAD+
-
Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
?
D-xylitol + NADP+ NADP+ is not a cofactor for wild-type, but for a substrate-binding loop chimera Deinococcus geothermalis ? + NADPH + H+
-
?

Synonyms

Synonyms Comment Organism
Dgeo_2865
-
Deinococcus geothermalis
PDH-11300
-
Deinococcus geothermalis
polyol dehydrogenase
-
Deinococcus geothermalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Deinococcus geothermalis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48.3
-
1 h, 50% residual activity, wild-type Deinococcus geothermalis
55.3
-
1 h, 50% residual activity, substrate-binding loop chimera Deinococcus geothermalis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.42
-
NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.53
-
NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.61
-
NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
2.7
-
NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Cofactor

Cofactor Comment Organism Structure
additional information no activity with NADPH Deinococcus geothermalis
NADH
-
Deinococcus geothermalis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.45
-
NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
3.48
-
NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
10.74
-
NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
17.8
-
NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis