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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
Search for more literature for 1.1.1.14

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