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Information on EC 1.1.1.48 - D-galactose 1-dehydrogenase
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1.1.1.48 D-galactose 1-dehydrogenaseIUBMB Comments
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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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
galdh, d-galactose dehydrogenase, beta-galactose dehydrogenase, d-galactose 1-dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-galactose dehydrogenase
D-galactose dehydrogenase
GALDH
NAD-dependent D-galactose dehydrogenase
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beta-galactose dehydrogenase
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D-galactose dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
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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
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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
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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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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
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-
-
?
3-deoxy-D-galactose + NAD+
3-deoxy-galactono-1,5-lactone + NADH
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-
-
?
4-deoxy-D-galactose + NAD+
4-deoxy-galactono-1,5-lactone + NAD(P)H
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-
-
?
D-galactopyranose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
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-
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?
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
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-
-
?
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
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-
-
?
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
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-
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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-
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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-
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?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
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?
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
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-
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D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
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-
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?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
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1 mM, better substrate than D-galactose
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
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-
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?
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
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?
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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)
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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
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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
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pH 7.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.32
D-galactose
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pH 8.0, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.37
D-galactose
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beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
0.4
D-galactose
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beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
0.43
D-galactose
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pH 8.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.45
D-galactose
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beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
0.43
L-arabinose
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pH 7.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.5
L-arabinose
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pH 8.0, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.68
L-arabinose
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pH 8.5, beta-galactosidase-galactose dehydrogenase fusion enzyme
0.25
NAD+
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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
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substrate combination L-arabinose and D-galactose, coenzyme NADP+, cell free extracts
0.009
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crude extracts, cells grown on D-galactose, inducible enzyme
0.023
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crude extracts, cells grown on D-galactose, inducible enzyme
0.026
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crude extracts, cells grown on D-galactose, inducible enzyme
0.071
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substrate combination L-arabinose and galactose, coenzyme NAD, cell free extracts
17
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beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
27
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beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
29
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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
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brenda
mutant strain, grows on galactose in the absence of dibutyryl cyclic AMP
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brenda
unable to grow on galactose as sole carbon source, growth occurs if dibutyryl cyclic AMP is added
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brenda
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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