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
-
hypothesise
-
hypocrea
-
aldo-keto
- erythritol
- gli1
- jecorina
- 1,3-dihydroxyacetone
-
bioproduction
-
iron-containing
-
enantiopure
- medicine
Reaction
Synonyms
AKR11B4, gamma-hydroxybutyrate dehydrogenase, glycerol dehydrogenase, GlyDH, Gox1615, NADP+-dependent glycerol dehydrogenase
ECTree
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General Information
General Information on EC 1.1.1.72 - glycerol dehydrogenase (NADP+)
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evolution
metabolism
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glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
-
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
-
evolution
-
glycerol dehydrogenases can be classified into three different groups. The first one, NAD+-dependent (EC 1.1.1.6), catalyzes the oxidation of glycerol to DHA. The second (EC 1.1.1.156), also named DHA reductase, oxidizes glycerol to DHA in the presence of nicotinamide adenine dinucleotide phosphate (NADP+). The third one (EC 1.1.1.72) transforms glycerol to D-glyceraldehyde in the presence of NADP+. The latter enzymes also use D-glyceraldehyde, or its stereoisomer, as substrate in a reverse reaction for producing glycerol, as in glycerolipid metabolism
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glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
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glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
-
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
-
metabolism
-
glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH (Km for DL-glyceraldehyde ranging from 12.8 to 32.3 mM). This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur, supporting the assumption that the main metabolic flux concerning glycerol metabolism is through the glycerol kinase pathway, but glycerol kinase is not completely controlling the flux of glycerol metabolism in the lactobacilli
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