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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.14 expression in Escherichia coli Deinococcus geothermalis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.14 D55N mutation located at the NAD+ binding cleft, changes cofactor specificity frm NADH to NADPH Deinococcus geothermalis
1.1.1.14 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.14 0.15
-
 NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 0.15
-
 NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 0.41
-
 NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 0.44
-
 NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.14 Deinococcus geothermalis Q1J2J0
-
-
1.1.1.14 Deinococcus geothermalis DSM 11300 Q1J2J0
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.14 936
-
 substrate D-sorbitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 1013
-
 substrate 1,2-butanediol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 1427
-
 substrate D-galactitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 2742
-
 substrate 1,2-hexanediol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 4659
-
 substrate D-xylitol, wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.14 1,2-butanediol + NAD+
-
 Deinococcus geothermalis ? + NADH + H+
-
 ?
1.1.1.14 1,2-butanediol + NAD+
-
 Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
 ?
1.1.1.14 1,2-hexanediol + NAD+
-
 Deinococcus geothermalis ? + NADH + H+
-
 ?
1.1.1.14 1,2-hexanediol + NAD+
-
 Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
 ?
1.1.1.14 D-galactitol + NAD+
-
 Deinococcus geothermalis D-tagatose + NADH + H+
-
 ?
1.1.1.14 D-galactitol + NAD+
-
 Deinococcus geothermalis DSM 11300 D-tagatose + NADH + H+
-
 ?
1.1.1.14 D-sorbitol + NAD+
-
 Deinococcus geothermalis L-sorbose + NADH + H+
-
 ?
1.1.1.14 D-sorbitol + NAD+
-
 Deinococcus geothermalis DSM 11300 L-sorbose + NADH + H+
-
 ?
1.1.1.14 D-xylitol + NAD+
-
 Deinococcus geothermalis ? + NADH + H+
-
 ?
1.1.1.14 D-xylitol + NAD+
-
 Deinococcus geothermalis DSM 11300 ? + NADH + H+
-
 ?
1.1.1.14 D-xylitol + NADP+ NADP+ is not a cofactor for wild-type, but for a substrate-binding loop chimera Deinococcus geothermalis ? + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.14 Dgeo_2865
-
 Deinococcus geothermalis
1.1.1.14 PDH-11300
-
 Deinococcus geothermalis
1.1.1.14 polyol dehydrogenase
-
 Deinococcus geothermalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.14 45
-
-
 Deinococcus geothermalis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.14 48.3
-
 1 h, 50% residual activity, wild-type Deinococcus geothermalis
1.1.1.14 55.3
-
 1 h, 50% residual activity, substrate-binding loop chimera Deinococcus geothermalis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.14 1.42
-
 NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 1.53
-
 NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 1.61
-
 NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 2.7
-
 NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis

Cofactor

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.14 3.45
-
 NADP+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 3.48
-
 NAD+ substrate-binding loop chimera plus mutation D55N, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 10.74
-
 NAD+ wild-type, pH 9.0, temperature not specified in the publication Deinococcus geothermalis
1.1.1.14 17.8
-
 NAD+ substrate-binding loop chimera, pH 9.0, temperature not specified in the publication Deinococcus geothermalis