1.1.1.72: glycerol dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about glycerol dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.72
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1.1.1.72
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polyols
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racemic
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oxydans
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gluconobacter
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l-glyceraldehyde
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stearothermophilus
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nadp-dependent
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nidulans
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enantioselectivity
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1.1.1.6
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hypothesise
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hypocrea
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aldo-keto
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erythritol
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gli1
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jecorina
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1,3-dihydroxyacetone
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bioproduction
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iron-containing
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enantiopure
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medicine
- 1.1.1.72
- polyols
-
racemic
- oxydans
-
gluconobacter
- l-glyceraldehyde
- stearothermophilus
-
nadp-dependent
- nidulans
-
enantioselectivity
-
1.1.1.6
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hypothesise
-
hypocrea
-
aldo-keto
- erythritol
- gli1
- jecorina
- 1,3-dihydroxyacetone
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bioproduction
-
iron-containing
-
enantiopure
- medicine
Reaction
Synonyms
AKR11B4, gamma-hydroxybutyrate dehydrogenase, glycerol dehydrogenase, GlyDH, Gox1615, NADP+-dependent glycerol dehydrogenase
ECTree
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KM Value
KM Value on EC 1.1.1.72 - glycerol dehydrogenase (NADP+)
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2.69
D-glyceraldehyde
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reduction, pH 7.0, 30°C, Vmax: 77.9 micromol/min/mg
12.8
D-glyceraldehyde
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reverse reaction, pH 6.5, 25°C, crude extract
20.2
D-glyceraldehyde
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reverse reaction, pH 6.5, 25°C, crude extract
32.3
D-glyceraldehyde
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reverse reaction, pH 6.5, 25°C, crude extract
additional information
KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C
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additional information
additional information
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KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C
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additional information
additional information
KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C
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additional information
additional information
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KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C
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additional information
additional information
KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C
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additional information
additional information
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KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C
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additional information
additional information
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enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
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additional information
additional information
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enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
-
additional information
additional information
-
enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models
-