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
-
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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Metals Ions
Metals Ions on EC 1.1.1.14 - L-iditol 2-dehydrogenase
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Zn
Zn2+
Zn2+
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1 catalytic zinc atom per subunit, interaction with Ser46 and the oxygen atom of the 2-hydroxy and the 4-hydroxy groups is important for substrate binding
Zn2+
the catalytic zinc is coordinated with residues His69, Cys44, Glu70, and a water molecule
Zn2+
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apparent stability constant of 1600000000000 per M for Zn(II)SDH. Under physiological conditions, enzyme is saturated with Zn2+