Information on EC 1.1.1.48 - D-galactose 1-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.48
-
RECOMMENDED NAME
GeneOntology No.
D-galactose 1-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-galactose + NAD+ = D-galactono-1,4-lactone + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactose degradation II
-
-
Galactose metabolism
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-
Metabolic pathways
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-54-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Caulobacter crescentus AE22
mutant strain, grows on galactose in the absence of dibutyryl cyclic AMP
-
-
Manually annotated by BRENDA team
Caulobacter crescentus AE23
mutant strain, grows on galactose in the absence of dibutyryl cyclic AMP
-
-
Manually annotated by BRENDA team
Caulobacter crescentus CB13
unable to grow on galactose as sole carbon source, growth occurs if dibutyryl cyclic AMP is added
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-
Manually annotated by BRENDA team
constitutive galactose dehydrogenase activity
-
-
Manually annotated by BRENDA team
constitutive galactose dehydrogenase activity
-
-
Manually annotated by BRENDA team
Rhizobium meliloti L5-30
-
-
-
Manually annotated by BRENDA team
galactose mutant
-
-
Manually annotated by BRENDA team
galactose mutant
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-galactose + NAD+
2-deoxy-galactono-1,5-lactone + NADH
show the reaction diagram
2-deoxy-D-galactose + NADP+
2-deoxy-galactono-1,5-lactone + NADPH
show the reaction diagram
-
-
-
?
3-deoxy-D-galactose + NAD+
3-deoxy-galactono-1,5-lactone + NADH
show the reaction diagram
-
-
-
?
4-deoxy-D-galactose + NAD+
4-deoxy-galactono-1,5-lactone + NAD(P)H
show the reaction diagram
-
-
-
?
6-deoxy-alpha-D-galactose + NAD+
6-deoxy-galactono-1,5-lactone + NADH
show the reaction diagram
D-galactopyranose + NAD(P)+
D-galactono-1,5-lactone + NAD(P)H
show the reaction diagram
-
-
-
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
show the reaction diagram
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
show the reaction diagram
succinate + NAD(P)+
succinic acid anhydride + NAD(P)H
show the reaction diagram
Rhizobium meliloti L5-30
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
show the reaction diagram
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
preferred cofactor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
p-chloromercuribenzoate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.185 - 1
D-galactose
0.215 - 0.68
L-arabinose
0.125 - 0.25
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
358 - 1180
D-galactose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0074
-
substrate combination L-arabinose and D-galactose, coenzyme NADP+, cell free extracts
0.008
Rhizobium meliloti L5-30
-
substrate succinate, coenzyme NADP+, cell free extracts
0.009
Caulobacter crescentus AE23
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.012
Rhizobium meliloti L5-30
-
substrate succinate, coenzyme NAD+, cell free extracts
0.023
Caulobacter crescentus AE22
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.026
Caulobacter crescentus CB13
-
crude extracts, cells grown on D-galactose, inducible enzyme
0.031
Rhizobium meliloti L5-30
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coenzyme NADP+, cell free extracts
0.036
Rhizobium meliloti L5-30
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coenzyme NAD+, cell free extracts
0.06
-
crude extracts, cells grown on sucrose
0.071
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substrate combination L-arabinose and galactose, coenzyme NAD, cell free extracts
0.078
Rhizobium meliloti L5-30
-
substrate L-arabinose, coenzyme NADP+, cell free extracts
0.079
Rhizobium meliloti L5-30
-
substrate L-arabinose, coenzyme NAD+, cell free extracts
0.42
-
cell 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
36
Rhizobium meliloti L5-30
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272
Rhizobium meliloti L5-30
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coenzyme NADP+
390
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substrate L-arabinose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
recombinant, purified
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhizobium etli (strain CFN 42 / ATCC 51251)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
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gel filtration
74000
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gel filtration
102000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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alpha,alpha, 2 * 32000, SDS-PAGE
tetramer
additional information
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structure modelling and computational analysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 9.2
-
-
286971
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 65
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5 min, 100% activity at 57°C, rapid drop above 60°C
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
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286969, 286972, 286973, 286974
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
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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
ammonium sulfate, CM-Sephadex, DEAE-Sephadex, hydroxyapatite, disc electrophoresis
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ammonium sulfate, DEAE-Sepharose, FPLC-Superose 12, beta-galactosidase-galactose dehydrogenase fusion enzyme
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ammonium sulfate, heat, phosphate precipitation, DEAE-cellulose, hydroxyapatite
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by affinity chromatography on chimeric mimodye-ligand gel resins, method evaluation
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Mono Q column, partially purified enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-galactosidase-galactose dehydrogenase fusion enzymes, expressed in Escherichia coli
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expressed in Escherichia coli, Escherichia coli beta-galactosidase promotor
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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 hide
LITERATURE
analysis
biotechnology
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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
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