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Information on EC 1.1.1.48 - D-galactose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.48
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.48 D-galactose 1-dehydrogenase
IUBMB Comments
This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
showSynonyms
galdh, d-galactose dehydrogenase, beta-galactose dehydrogenase, d-galactose 1-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-galactose dehydrogenase
D-galactose dehydrogenase
GALDH
NAD-dependent D-galactose dehydrogenase
-
-
-
-
beta-galactose dehydrogenase
-
-
-
-
D-galactose dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
-
-
-
-
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
B-type enzyme with regard to stereochemistry, transfers hydrogen from carbon-1 of D-galactose to si face of NAD, in the reverse reaction the pro-S hydrogen atom from carbon-4 of NAD(P)H is transferred to the re face of carbon-1 of D-galactono-1,5-lactone
-
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
B-type enzyme with regard to stereochemistry, transfers hydrogen from carbon-1 of D-galactose to si face of NAD, in the reverse reaction the pro-S hydrogen atom from carbon-4 of NAD(P)H is transferred to the re face of carbon-1 of D-galactono-1,5-lactone
-
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
depending on the pH, the immediately formed D-galactono-1,5-lactone rearranges intramolecularly to the corresponding 1,4-lactone or hydrolyzes to D-galctonate or both
-
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
depending on the pH, the immediately formed D-galactono-1,5-lactone rearranges intramolecularly to the corresponding 1,4-lactone or hydrolyzes to D-galctonate or both
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-galactose:NAD+ 1-oxidoreductase
This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose.
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CAS REGISTRY NUMBER
COMMENTARY
9028-54-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-galactose + NADP+
2-deoxy-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
3-deoxy-D-galactose + NAD+
3-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
4-deoxy-D-galactose + NAD+
4-deoxy-galactono-1,5-lactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
D-galactopyranose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
succinate + NAD(P)+
succinic acid anhydride + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
286955, 286956, 286957, 286958, 286959, 286960, 286962, 286963, 286964, 286966, 286967, 286969, 286970, 286971
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: 1 mM, better substrate than D-galactose
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
286955, 286956, 286957, 286958, 286959, 286960, 286962, 286963, 286964, 286966, 286967, 286969, 286970, 286971
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
reacts with first 4 sulfhydryl groups of enzyme, inhibition is completely reversible upon addition of reducing agents, NAD+ and NADH protect against inactivation
anthraquinone-diamino-benzosulfonyl-dichlorotriazine
-
i.e. Vilmafix Blue A-R, and other derivatives of longer side chain length, inactivation, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Galactosemias
Expression and response surface optimization of the recovery and purification of recombinant D-galactose dehydrogenase from Pseudomonas fluorescens.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
D-galactose
-
pH 7.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.32
D-galactose
-
pH 8.0, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.37
D-galactose
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
0.4
D-galactose
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
0.43
D-galactose
-
pH 8.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.45
D-galactose
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
0.43
L-arabinose
-
pH 7.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.5
L-arabinose
-
pH 8.0, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.68
L-arabinose
-
pH 8.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.25
NAD+
-
beta-galactosidase-galactose dehydrogenase fusion enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0074
-
substrate combination L-arabinose and D-galactose, coenzyme NADP+, cell free extracts
0.009
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.023
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.026
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.071
-
substrate combination L-arabinose and galactose, coenzyme NAD, cell free extracts
17
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
27
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
29
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
76
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutant strain, grows on galactose in the absence of dibutyryl cyclic AMP
-
-
brenda
mutant strain, grows on galactose in the absence of dibutyryl cyclic AMP
-
-
brenda
unable to grow on galactose as sole carbon source, growth occurs if dibutyryl cyclic AMP is added
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (316 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
26000
-
alpha4, 4 * 26000, 100 mM phosphate buffer, pH 7.4, 8 M urea, 100 mM 2-mercaptoethanol, sedimentation equilibrium
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
structure modelling and computational analysis
tetramer
-
alpha4, 4 * 26000, 100 mM phosphate buffer, pH 7.4, 8 M urea, 100 mM 2-mercaptoethanol, sedimentation equilibrium
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
-
native enzyme, 70% activity after 20 min, 30% after 60 min, 20% after 90 min, beta-galactosidase-galactose dehydrogenase fusion enzymes, 80% activity after 90 min
50
-
50% activity after 60 min, 100 mM, pH 8.0, 1 mM MgCl2, 1 mM dithiothreitol
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation of sulhydryl residues inactivates enzyme, reactivation with 100 mM 2-mercaptoethanol or 10 mM dithiothreitol, pH 7.0, 30°C, enzymatically active oligomers of native enzyme are formed upon storage without reducing agents
-
286969, 286972, 286973, 286974
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 100 mM phosphate buffer, pH 6.5-7.6, 30-50% glycerol, 18 months, no loss of activity
-
4°C, 3.5 M (NH4)2SO4, 20 mM 2-mercaptoethanol, pH 7.0, several months, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
12% (w/v) ammonium sulfate precipitation and 14% (w/v) polyethylene glycol 2000 precipitation at pH 7.5
-
ammonium sulfate, CM-Sephadex, DEAE-Sephadex, hydroxyapatite, disc electrophoresis
-
ammonium sulfate, DEAE-Sepharose, FPLC-Superose 12, beta-galactosidase-galactose dehydrogenase fusion enzyme
-
ammonium sulfate, heat, phosphate precipitation, DEAE-cellulose, hydroxyapatite
-
aqueous two-phase system composed of 12% (w/v) PEG-6000, 15% (w/v) K2HPO4 with pH 7.5 at 25°C
-
by affinity chromatography on chimeric mimodye-ligand gel resins, method evaluation
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-galactosidase-galactose dehydrogenase fusion enzymes, expressed in Escherichia coli
-
expressed in Escherichia coli, Escherichia coli beta-galactosidase promotor
-
expressed in Escherichia coli, point mutations in natural promotor increase expression
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stress treatments, e.g. chilling, heat shock, or high light intensity, enhance L-GalDH-RNA level in leaves
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
design and synthesis by protein molecular modelling and ligand docking of several chimeric mimodye-ligands comprising a NAD-pseudomimetic moiety of anthraquinone diaminobenzosulfonic acid and a galactosyl-mimetic moiety of 2-amino-2-deoxygalactose or shikimic acid for usage as tailored ligands in selective affinity chromatography during enzyme purification/production, immobilization on a gel resin, overview
analysis
-
determination of lactose using a biosensor made of immobilized beta-galctosidase-galactose dehydrogenase fusion enzyme
analysis
-
determination of galactose in various hepatic diseases and galactosaemia in clinical biochemistry
analysis
-
determination of galactose in various hepatic diseases and galactosaemia in clinical biochemistry
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurn, N.; Contreras, I.; Shapiro, L.
Galactose catabolism in Caulobacter crescentus
J. Bacteriol.
135
517-520
1978
Caulobacter crescentus AE22, Caulobacter crescentus AE23, Caulobacter crescentus CB13
brenda
Arias, A.; Cervenansky, C.
Galactose metabolism in Rhizobium meliloti L5-30
J. Bacteriol.
167
1092-1094
1986
Rhizobium meliloti L5-30, Sinorhizobium meliloti, Sinorhizobium meliloti UR23
brenda
Hu, A.S.L.; Cline, A.L.
The regulation of some sugar dehydrogenases in a Pseudomonad
Biochim. Biophys. Acta
93
237-245
1964
Pseudomonas sp., Pseudomonas sp. G6
brenda
Carlsson, H.; Ljung, S.; Bulow, L.
Physical and kinetic effects on introduction of various linker regions in beta-galactosidase/galactose dehydrogenase fusion enzymes
Biochim. Biophys. Acta
1293
154-160
1996
Pseudomonas fluorescens
brenda
Carlsson, H.; Ljungcrantz, P.; Lindbladh, C.; Persson, M.; Bulow, L.
Use of geneticallly prepared enzyme conjugates in lactose and galactose analyses
Anal. Biochem.
218
278-283
1994
Pseudomonas fluorescens
brenda
Wong, T.Y.; Yao, X.T.
The deLey-Doudoroff pathway of galactose metabolism in Azotobacter vinelandii
Appl. Environ. Microbiol.
60
2065-2068
1994
Azotobacter vinelandii, Pelomonas saccharophila, Pseudomonas fluorescens, Rhizobium meliloti L5-30
brenda