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Information on EC 1.1.1.120 - galactose 1-dehydrogenase (NADP+)
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1.1.1.120 galactose 1-dehydrogenase (NADP+)IUBMB Comments
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
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Word Map
- 1.1.1.120
- nad+
-
azospirillum
-
non-phosphorylating
-
nadp+-dependent
- brasilense
- dehydrogenases
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aradh, nadp-galactose-1-dehydrogenase, l-arabinose/d-galactose 1-dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-galactose dehydrogenase (NADP+)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
D-galactose:NADP+ 1-oxidoreductase
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
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CAS REGISTRY NUMBER
COMMENTARY
37250-51-4
-
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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
2,6-dideoxy-D-allofuranose + NADP+
? + NADPH
-
i.e. digitoxose, furanose form, 81% of the activity compared to abequose
-
?
2,6-dideoxy-D-allose + NADP+
?
-
81% activity compared to 3,6-dideoxy-D-galactose
-
-
r
2-deoxy-D-ribose + NADP+
? + NADPH
-
18% of the activity compared to abequose
-
?
3,6-dideoxy-beta-D-galactofuranose + NADP+
3,6-dideoxy-D-galactono-1,4-lactone + NADPH
-
i.e. abequose, furanose form, beta-configuration
-
?
3-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
36% of the activity compared to abequose
-
?
alpha-D-galactose + NADP+
D-galactonolactone + NADPH
-
39% of the activity compared to alpha,beta-D-galactose and alpha,beta-L-arabinose
product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactose + NADP+
D-galatonolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
D-arabinose + NADP+
D-arabinolactone + NADPH
-
5% of the activity compared to abequose
-
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
-
-
-
-
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
-
69% activity compared to D-fucose
-
-
?
L-arabinose + NAD+
L-arabino-1,5-lactone + NADH + H+
-
-
-
-
?
L-arabinose + NADP+
?
-
12% activity compared to D-fucose
-
-
?
L-arabinose + NADP+
L-arabinolactone + NADPH
-
6% of the compared to abequose
-
?
additional information
?
-
-
some minor activity (about 1%) can be measured with D-xylose and L-lyxose, while no activity is detected with D-glucose or L-rhamnose
-
-
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
114% of the activity compared to abequose
-
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
90% of the activity compared to D-galactose
product is assumed to be the corresponding -1,5-lactone
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
90% of the activity compared to D-galactose
product is assumed to be the corresponding -1,5-lactone
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
94% of the activity compared to abequose
-
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
156% of the activity compared to D-galactose
product is assumed to be the corresponding -1,5-lactone
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
156% of the activity compared to D-galactose
product is assumed to be the corresponding -1,5-lactone
?
alpha,beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
alpha,beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
furanose form, beta-configuration
-
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
-
-
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
-
-
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
63% of the activity compared to alpha,beta-L-arabinose and alpha,beta-D-galactose
product is assumed to be the corresponding -1,5-lactone
?
beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
63% of the activity compared to alpha,beta-L-arabinose and alpha,beta-D-galactose
product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
furanose form, beta-configuration
gamma-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
L-arabinose + NADP+
L-arabino-1,5-lactone + NADPH + H+
-
44% of the activity compared to D-galactose
product is assumed to be the corresponding -1,5-lactone
?
L-arabinose + NADP+
L-arabino-1,5-lactone + NADPH + H+
-
21% activity compared to D-fucose
-
-
?
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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
alpha-D-galactose + NADP+
D-galactonolactone + NADPH
-
39% of the activity compared to alpha,beta-D-galactose and alpha,beta-L-arabinose
product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactose + NADP+
D-galatonolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
furanose form, beta-configuration
gamma-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
-
product is assumed to be the corresponding -1,5-lactone
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the enzyme prefers NADP+ but uses also NAD+ as a cofactor
NADP+
-
the enzyme prefers NADP+ but uses also NAD+ as a cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
complete inhibition at 1 mM, partial reversible by low concentration of cysteine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.48
D-galactose
-
with NAD+ as cosubstrate, at pH 9.0 and 23°C
0.5
D-galactose
-
with NADP+ as cosubstrate, at pH 9.0 and 23°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
38.12
D-galactose
-
with NAD+ as cosubstrate, at pH 9.0 and 23°C
69.9
D-galactose
-
with NADP+ as cosubstrate, at pH 9.0 and 23°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
80.17
D-galactose
-
with NAD+ as cosubstrate, at pH 9.0 and 23°C
140
D-galactose
-
with NADP+ as cosubstrate, at pH 9.0 and 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLCDH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
361
0
40250
Swiss-Prot
-
A0A1J5P6Y4_9ZZZZ
228
0
25247
TrEMBL
other Location (Reliability: 3)
A0A7Z7J4V1_XANCH
311
0
33932
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, ammonium sulfate precipitate, many months, without appreciable loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity increases at the beginning of salt stress, up to 3.6fold increase. Hypoosmotic stress does not induce the activity
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cline, A.L.; Hu, A.S.L.
The isolation of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4488-4492
1965
Pseudomonas sp.
brenda
Cline, A.L.; Hu, A.S.L.
Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4493-4497
1965
Pseudomonas sp.
brenda
Schiwara, H.W.; Domagk, G.F.
Anreicherung und Charakterisierung einer NADP+-abhngigen Abequosedehydrogenase aus Pseudomonas putida
Hoppe-Seyler's Z. Physiol. Chem.
349
1321-1329
1968
Pseudomonas putida
brenda
Aro-Kaerkkaeinen, N.; Toivari, M.; Maaheimo, H.; Ylilauri, M.; Pentikaeinen, O.T.; Andberg, M.; Oja, M.; Penttilae, M.; Wiebe, M.G.; Ruohonen, L.; Koivula, A.
L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
98
9653-9665
2014
Rhizobium leguminosarum bv. trifolii
brenda
Hyskova, V.; Pliskova, V.; Cerveny, V.; Ryslava, H.
NADP-dependent enzymes are involved in response to salt and hypoosmotic stress in cucumber plants
Gen. Physiol. Biophys.
36
247-258
2017
Cucumis sativus
brenda
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