1.1.1.14: L-iditol 2-dehydrogenase
This is an abbreviated version!
For detailed information about L-iditol 2-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.14
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1.1.1.14
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polyols
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aminotransferase
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aldose
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hepatotoxicity
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fructose
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necrosis
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transaminase
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dehydrogenases
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bile
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lens
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alt
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sheep
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bilirubin
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gamma-glutamyl
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testicular
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cataract
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transpeptidase
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gluconobacter
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ccl4
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acetaminophen
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tetrachloride
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centrilobular
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xylitol
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oxydans
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hepatoprotective
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galactitol
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apap
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ribitol
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acetaminophen-induced
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diapause
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pneumotoxicity
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bromobenzene
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13-week
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n-demethylase
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d-mannitol
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forestomach
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hepatotoxicants
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fructokinase
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l-sorbose
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aminopyrine
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glutamic-pyruvic
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sorbinil
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medicine
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agriculture
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synthesis
- 1.1.1.14
- polyols
- aminotransferase
- aldose
-
hepatotoxicity
- fructose
- necrosis
- transaminase
- dehydrogenases
- bile
- lens
-
alt
- sheep
- bilirubin
-
gamma-glutamyl
- testicular
- cataract
- transpeptidase
- gluconobacter
- ccl4
- acetaminophen
-
tetrachloride
-
centrilobular
- xylitol
- oxydans
-
hepatoprotective
- galactitol
- apap
- ribitol
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acetaminophen-induced
-
diapause
-
pneumotoxicity
- bromobenzene
-
13-week
- n-demethylase
- d-mannitol
-
forestomach
-
hepatotoxicants
- fructokinase
- l-sorbose
- aminopyrine
-
glutamic-pyruvic
- sorbinil
- medicine
- agriculture
- synthesis
Reaction
Synonyms
ADH, D-sorbitol dehydrogenase, dehydrogenase, L-iditol, Dgeo_2865, glucitol dehydrogenase, GoSCR, L-iditol 2-dehydrogenase, L-iditol dehydrogenase (sorbitol), L-iditol:NAD oxidoreductase, L-iditol:NAD+ 5-oxidoreductase, LeSDH, MdSDH5, More, NAD+-dependent sorbitol dehydrogenase, NAD-dependent polyol dehydrogenase, NAD-dependent sorbitol dehydrogenase, NAD-SDH, NAD-sorbitol dehydrogenase, PDH-11300, polyol dehydrogenase, Protein tms1, SDH, SldA, SLDH, SOR, Sor1, Sor2, sorbitol dehydrogenase, sorbitol dehydrogenase 1, sorbitol dehydrogenase 2, sorbitol related enzyme, SORD
ECTree
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Engineering
Engineering on EC 1.1.1.14 - L-iditol 2-dehydrogenase
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E154C
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purified preparations of mutant contain 0.1-0.4 atoms of Zn2+ per subunit and exhibit a constant catalytic Zn2+ centre activity of 1.19 per s, mutant does not require exogenous Zn2+ for stability. Mutant retains less than 1% of wild-type catalytic efficiency and displays similar primary and solvent deuterium effects as wild-type
D55N
D364A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
H302A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
M366A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
Y110F
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mutation in hydrogen onding network, complete loss of activity and destabilization of protein into tetramers, dimers and monomers compared to only tetramers for wild-type
additional information
mutation located at the NAD+ binding cleft, changes cofactor specificity frm NADH to NADPH
D55N
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mutation located at the NAD+ binding cleft, changes cofactor specificity frm NADH to NADPH
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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
additional information
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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
additional information
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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
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additional information
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construction of disruption mutants of genes sldA or sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA
additional information
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construction of gene disruption mutants of genes sldA and sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA, co-expression of sldB is required for enzyme activity in vivo
additional information
in vitro bioreduction of 2-hydroxyacetophenone (2-HAP) is catalyzed by GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration. The two coexpressed enantiocomplementary carbonyl reductases, BDHA (2, 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, method optimization, overview. Products (R)-PED and (S)-PED are obtained with 99% yield, over 99% enantiomeric excess and 18.0 g/l/h volumetric productivity. The reaction is carried out in 5 ml sodium phosphate buffer (pH 7.0, 100 mM) at 30°C, containing 10 U/ml BDHA (cell free extract of Escherichia coli (BDHA)), 15 U/ml GoSCR (cell free extract of Escherichia coli (GoSCR)), 10 U/ml GDH (cell free extract of Escherichia coli (GDH)), 50-200 mM 2-HAP (with 10% DMSO as cosolvent), 60-250 mM D-glucose. Strong tolerance of BDHA and GoSCR against high substrate concentration
additional information
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in vitro bioreduction of 2-hydroxyacetophenone (2-HAP) is catalyzed by GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration. The two coexpressed enantiocomplementary carbonyl reductases, BDHA (2, 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, method optimization, overview. Products (R)-PED and (S)-PED are obtained with 99% yield, over 99% enantiomeric excess and 18.0 g/l/h volumetric productivity. The reaction is carried out in 5 ml sodium phosphate buffer (pH 7.0, 100 mM) at 30°C, containing 10 U/ml BDHA (cell free extract of Escherichia coli (BDHA)), 15 U/ml GoSCR (cell free extract of Escherichia coli (GoSCR)), 10 U/ml GDH (cell free extract of Escherichia coli (GDH)), 50-200 mM 2-HAP (with 10% DMSO as cosolvent), 60-250 mM D-glucose. Strong tolerance of BDHA and GoSCR against high substrate concentration
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additional information
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construction of disruption mutants of genes sldA or sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA
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additional information
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construction of gene disruption mutants of genes sldA and sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA, co-expression of sldB is required for enzyme activity in vivo
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