Information on EC 1.1.1.72 - glycerol dehydrogenase (NADP+)

Substrates: -
Products: -

glycolaldehyde + NADPH

ethyleneglycol + NADP+

Substrates: -
Products: -

glycolaldehyde + NADPH

ethyleneglycol + NADP+

Substrates: -
Products: -

hexanal + NADPH + H+

hexanol + NADP+

Substrates: reduction reaction. Specific activity: 31.9 micromol/min/mg
Products: -

hexanal + NADPH + H+

hexanol + NADP+

711534

Substrates: -
Products: -

hexane-1,2,6-triol + NADP+

? + NADPH

Substrates: oxidation reaction. Specific activity: 0.3 micromol/min/mg
Products: -

hexane-1,2,6-triol + NADP+

? + NADPH

Substrates: oxidation reaction. Specific activity: 0.45 micromol/min/mg
Products: -

L-glyceraldehyde + NADPH

glycerol + NADP+

Substrates: 36% of D-glyceraldehyde activity
Products: -

L-glyceraldehyde + NADPH

glycerol + NADP+

Substrates: -
Products: -

methylglyoxal + NADPH

1-hydroxyacetone + NADP+

Substrates: -
Products: -

methylglyoxal + NADPH

1-hydroxyacetone + NADP+

Substrates: -
Products: -

methylglyoxal + NADPH

1-hydroxyacetone + NADP+

287283, 287286

Substrates: -
Products: -

n-butyraldehyde + NADPH

n-butanol + NADP+

Substrates: -
Products: -

n-butyraldehyde + NADPH

n-butanol + NADP+

Substrates: -
Products: -

n-pentanal + NADPH + H+

n-pentanol + NADP+

Substrates: -
Products: -

n-pentanal + NADPH + H+

n-pentanol + NADP+

Substrates: -
Products: -

propionaldehyde + NADPH

propanol + NADP+

Substrates: -
Products: -

propionaldehyde + NADPH

propanol + NADP+

Substrates: -
Products: -

additional information

Substrates: the enzyme is part of the biosynthetic pathway for glycerol
Products: -

additional information

Substrates: glycerol dehydrogenase activity is detected in all Lactobacillus strains studied but only for the reduction of glyceraldehyde with NADPH. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
Products: -

additional information

additional information

Substrates: glycerol dehydrogenase activity is detected in all Lactobacillus strains. This enzyme shows a very low oxidative activity with glycerol and NADP+ and, most likely, under physiological conditions, the oxidative reaction does not occur
Products: -

additional information

additional information

Substrates: 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
Products: -

additional information

additional information

Substrates: no substrates: D-fructose, D-ribose, D-xylose
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

4 entries

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

dihydroxyacetone + NADPH + H+

Substrates: The enzyme plays a role in the glycerol biosynthesis during growth and in osmotolerance. The glycerol biosynthesis by enzyme is required for germination at high osmolarity.
Products: -

additional information

7 entries

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

Fusarium oxysporum

287284

Substrates: -
Products: -

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

Substrates: -
Products: -

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

Substrates: -
Products: -

D-glyceraldehyde + NADPH + H+

glycerol + NADP+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

glycerol + NADP+

D-glyceraldehyde + NADPH + H+

Substrates: -
Products: -

additional information

Substrates: the enzyme is part of the biosynthetic pathway for glycerol
Products: -

additional information

additional information

additional information

additional information

additional information

additional information

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NADH

NADP+

10 entries

NADPH

11 entries

NADH

10% of NADPH-activity

287283, 287286

NADH

NADP+

NADP+

NADP+

NADP+

NADP+

NADP+

NADP+

NADP+

NADP+

NADP+

NADPH

NADPH

NADPH

NADPH

NADPH

NADPH

NADPH

NADPH

prefers NADPH over NADH. Using NADPH, a 200fold increase in activity compared to the activity achieved with the same concentration of NADH is observed

NADPH

NADPH

NADPH

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

HCO3-

activates conversion of glycerol to dihydroxyacetone

287290

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

Diphenylhydantoin

fluoride

formononetin 7-O-glucoside

Mn2+

Na+

NADPH

inhibition if concentration is above 0.15 mM

p-chloromercuribenzoate

p-hydroxymercuribenzoate

Phenobarbitol

Urea

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NaCl

The presence of 1 M NaCl results in a significant increase in activity in the wild-type strain.

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

186

D-glucuronate

0.04 - 32.3

D-glyceraldehyde

7 entries

10 - 143

glycerol

193

L-arabitol

oxidation, pH 9.7, 37°C, Vmax: 8.67 micromol/min/mg

0.0125 - 0.056

NADP+

3 entries

0.0041 - 0.04

NADPH

7 entries

additional information

9 entries

0.04

D-glyceraldehyde

0.15

D-glyceraldehyde

2.69

D-glyceraldehyde

reduction, pH 7.0, 30°C, Vmax: 77.9 micromol/min/mg

11.5

D-glyceraldehyde

12.8

D-glyceraldehyde

reverse reaction, pH 6.5, 25°C, crude extract

20.2

D-glyceraldehyde

reverse reaction, pH 6.5, 25°C, crude extract

32.3

D-glyceraldehyde

reverse reaction, pH 6.5, 25°C, crude extract

glycerol

143

glycerol

0.0125

NADP+

0.02

NADP+

oxidation, pH 9.7, 37°C, Vmax: 2.1 micromol/min/mg

0.056

NADP+

0.0041

NADPH

wild-type protein, pH 7.0, 30°C

0.0062

NADPH

W23M mutant protein, pH 7.0, 30°C

0.0062

NADPH

W23A mutant protein, pH 7.0, 30°C

0.0067

NADPH

0.016

NADPH

0.024

NADPH

0.04

NADPH

reduction, pH 7.0, 30°C, Vmax: 101 micromol/min/mg

additional information

KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C

additional information

KM-value 2.4 mM with substrate DL-glyceraldehyde, wild-type protein, pH 7.0, 30°C

additional information

KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C

additional information

KM-value 49.4 mM with substrate DL-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C

additional information

KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C

additional information

KM-value 118.0 mM with substrate DL-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C

additional information

enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models

additional information

enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models

additional information

enzyme kinetic parameters are determined by fitting the initial rates to irreversible single substrate Michaelis-Menten models

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.7 - 57.2

NADPH

3 entries

additional information

2.7

NADPH

W23A mutant protein, pH 7.0, 30°C

35.4

NADPH

W23M mutant protein, pH 7.0, 30°C

57.2

NADPH

wild-type protein, pH 7.0, 30°C

additional information

52.8/sec with substrate D/L-glyceraldehyde, wild-type protein, pH 7.0, 30°C

additional information

52.8/sec with substrate D/L-glyceraldehyde, wild-type protein, pH 7.0, 30°C

additional information

24.2/sec with substrate D/L-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C

additional information

24.2/sec with substrate D/L-glyceraldehyde, W23M mutant protein, pH 7.0, 30°C

additional information

3.2/sec with substrate D/L-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C

additional information

3.2/sec with substrate D/L-glyceraldehyde, W23A mutant protein, pH 7.0, 30°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.4

NADPH

pH 7.0, 30 °C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0043

cell-free enzyme extract, reverse reaction, pH 6.5, 25°C

0.0049

cell-free enzyme extract, reverse reaction, pH 6.5, 25°C

0.0131

cell-free enzyme extract, reverse reaction, pH 6.5, 25°C

0.259

during growth on wheat grains at water activity at the time of harvest 1.00

0.517

during growth on wheat grains at water activity at the time of harvest 0.97

0.582

during growth on wheat dough at water activity at the time of harvest 0.98

1.034

during growth on wheat dough at water activity at the time of harvest 0.96

20.7

22.3

glyceraldehyde, crude extract of expressing Escherichia coli, pH not specified in the publication, temperature not specified in the publication

24.1

32.5

W23M mutant protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C

4.2

W23A mutant protein, NADPH as variable substrate, pH 7.0, 30°C

4.9

W23A mutant protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C

5.75

W23M mutant protein, NADPH as variable substrate, pH 7.0, 30°C

80.5

wild-type protein, DL-glyceraldehyde as variable substrate, pH 7.0, 30°C

87.1

wild-type protein, NADPH as variable substrate, pH 7.0, 30°C

additional information

additional information

comparison of activity in the wild-type and two gldB disruption strains. The presence of 1 M NaCl results in a significant increase in activity in the wild-type strain. In the gldB disruptions hardly any activity is detected.

additional information

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.8

D-glyceraldehyde reduction

5 - 7

5.4

D-glyceraldehyde reduction

5.5

optimal activity for reduction

6.5

9.5

glycerol oxidation

9.7

oxidation assay at

glycerol oxidation

glycerol oxidation

optimal pH for axidation

assay at, forward reaction

assay at, forward reaction

assay at, forward reaction

6.5

assay at, reverse reaction

6.5

assay at, reverse reaction

6.5

assay at, reverse reaction

6.5

D-glyceraldehyde reduction

reduction assay at

DL-glyceraldehyde reduction

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3 entries

reduction assay at

oxidation assay at

optimal activity

assay at, forward reaction

assay at, forward reaction

assay at, forward reaction

show all columns Go to Pi Value Search

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

Aspergillus ochraceus

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

SwissProt

brenda

711534, 711743

brenda

Uniprot

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

additional information

skeletal muscle

brenda

skeletal muscle

brenda

additional information

biodiesel-derived glycerol is used as the main carbon and energy source in batch microaerobic growth, the tested strains are able to assimilate glycerol, consuming between 38-48% in approximately 24 h. The strains catabolize glycerol mainly through glycerol kinase, EC 2.7.1.30. Glycerol dehydrogenase activity is also detected in the strains studied but only for the reduction of glyceraldehyde with NADPH

brenda

additional information

brenda

additional information

brenda

additional information

brenda

additional information

brenda

additional information

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

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

evolution

evolution

evolution

evolution

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

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

metabolism

metabolism

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

P55804 pBLAST

DHGP_ASPNG

10672

Swiss-Prot

Show Sequence

Q5FQJ0 pBLAST

Q5FQJ0_GLUOX

Gluconobacter oxydans (strain 621H)

332

37213

TrEMBL

Show Sequence

Q7Z8L1 pBLAST

Q7Z8L1_EMEND

Emericella nidulans

325

36981

TrEMBL

Show Sequence

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

160000

gel filtration

34000

gel filtration

287283, 287286

36980

calculated from amino acid sequence

37210

calculated from cDNA

37213

37213, calculated

38000

39000

show all columns Go to Subunit Search

SDS-PAGE

43000

x * 43000, SDS-PAGE

38000

SDS-PAGE

38000

SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 43000, SDS-PAGE

monomer

monomer

1 * 38000, SDS-PAGE

monomer

1 * 38000, SDS-PAGE

monomer

1 * 39000, SDS-PAGE

monomer

37213, calculated

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting-drop variant of the vapor diffusion method

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

W23A

W23 is a key residue (accelerator) for NADP/NADPH turnover

W23M

W23 is a key residue (accelerator) for NADP/NADPH turnover

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5 - 9.7

enzyme is stable and shows a residual activity of at least 82%

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4 - 30

stable between

the half-life of 25 min increases to 45 min upon addition of 400 mM glycerol

rapid inactivation occurs

5 min, 98% loss of activity

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

partially inactivated by freezing and thawing

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C or 4°C, purified enzyme stable for at least 3 months

-20°C, 1 year

-20°C, dialyzed against distilled H2O with 30 mg/ml polyethyleneglycol, or lyophilized, stable

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

partial purification

using Ni-NTA chromatography

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli BL21(DE3)

711534

His-tagged version

overexpressed in Escherichia coli as a His-tagged fusion protein

show all columns Go to Application Search

the gene gldB

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

Aspergillus ochraceus

NADP(+)-dependent glycerol dehydrogenase homologous protein is a major allergen. Glycerol dehydrogenase shows IgE reactivity amongst the selected atopic patient cohort. All together, 10 cross-reactive IgE-binding proteins are detected

761748

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Flynn, T.G.; Cromlish, J.A.

Glycerol dehydrogenase from rabbit muscle

Methods Enzymol.

237-242

1982

Oryctolagus cuniculus

7144572

brenda

287284

Castro, I.M.; Loureiro-Dias, M.C.

Glycerol utilization in Fusarium oxysporum var. lini: regulation of transport and metabolism

J. Gen. Microbiol.

137

1497-1502

1991

Fusarium oxysporum

1955848

brenda

Viswanath-Reddy, M.; Pyle, J.E.; Branch Howe, E.

Purification and properties of NADP+ -linked glycerol dehydrogenase from Neurospora crassa

J. Gen. Microbiol.

107

289-296

1978

Neurospora crassa

brenda

Kormann, A.W.; Hurst, R.O.; Flynn, T.G.

Purification and properties of an NADP+ -dependent glycerol dehydrogenase from rabbit skeletal muscle

Biochim. Biophys. Acta

258

40-55

1972

Oryctolagus cuniculus

4400494

brenda

Toews, C.J.

The kinetics and reaction mechanism of the nicotinamide-adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle

Biochem. J.

105

1067-1073

1967

Rattus norvegicus

16742532

brenda

287288

Walton, D.J.

Stereochemistry of reduction of D-glyceraldehyde catalyzed by a nicotinamide adenine dinucleotide phosphate dependent dehydrogenase from skeletal muscle

Biochemistry

3472-3478

1973

Oryctolagus cuniculus

4147215

brenda

Schuurink, R.; Busink, R.; Hondmann, D.H.A.; Witteveen, C.F.B.; Visser, J.

Purification and properties of NADP(+)-dependent glycerol dehydrogenases from Aspergillus nidulans and A. niger

J. Gen. Microbiol.

136

1043-1050

1990

Aspergillus nidulans, Aspergillus niger

2200840

brenda

287290

Inayat, M.S.; Mattey, M.

Regulation of NADP+-specific glycerol dehydrogenase in Aspergillus niger by bicarbonate ions

Biochem. Soc. Trans.

976-977

1988

Aspergillus niger

brenda

287291

Sealy-Lewis H.M.; Fairhurst V.

An NADP+-dependent glycerol dehydrogenase in Aspergillus nidulans is inducible by D-galacturonate

Curr. Genet.

293-296

1992

Aspergillus nidulans

1394511

brenda

Ruijter, G.J.G.; Visser, J.; Rinzema, A.

Polyol accumulation by Aspergillus oryzae at low water activity in solid-state fermentation

Microbiology

150

1095-1101

2004

Aspergillus oryzae

15073319

brenda

de Vries, R.P.; Flitter, S.J.; van de Vondervoort, P.J.; Chaveroche, M.K.; Fontaine, T.; Fillinger, S.; Ruijter, G.J.; d'Enfert, C.; Visser, J.

Glycerol dehydrogenase, encoded by gldB is essential for osmotolerance in Aspergillus nidulans

Mol. Microbiol.

131-141

2003

Aspergillus nidulans (Q7Z8L1), Aspergillus nidulans

12823816

brenda

711534

Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Weckbecker, A.; Eggert, T.; Hummel, W.

Characterization of a whole-cell catalyst co-expressing glycerol dehydrogenase and glucose dehydrogenase and its application in the synthesis of L-glyceraldehyde

Biotechnol. Bioeng.

106

541-552

2010

Gluconobacter oxydans

20198657

brenda

Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Eggert, T.; Hummel, W.

Characterisation of a recombinant NADP-dependent glycerol dehydrogenase from Gluconobacter oxydans and its application in the production of L-glyceraldehyde

ChemBioChem

1888-1896

2009

Gluconobacter oxydans

19579248

brenda

Richter, N.; Breicha, K.; Hummel, W.; Niefind, K.

The Three-Dimensional Structure of AKR11B4, a Glycerol Dehydrogenase from Gluconobacter oxydans, Reveals a Tryptophan Residue as an Accelerator of Reaction Turnover

J. Mol. Biol.

404

353-362

2010

Gluconobacter oxydans (Q5FQJ0), Gluconobacter oxydans

20887732

brenda