Any feedback?
No. of entries
Information on EC 1.1.1.120 - galactose 1-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.120
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.120 galactose 1-dehydrogenase (NADP+)
IUBMB Comments
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.120
- nad+
-
azospirillum
-
non-phosphorylating
-
nadp+-dependent
- brasilense
- dehydrogenases
showSynonyms
aradh, nadp-galactose-1-dehydrogenase, l-arabinose/d-galactose 1-dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-galactose dehydrogenase (NADP+)
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-galactose:NADP+ 1-oxidoreductase
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-51-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-dideoxy-D-allofuranose + NADP+
? + NADPH
-
Substrates: i.e. digitoxose, furanose form, 81% of the activity compared to abequose
Products: -
Products: -
?
2,6-dideoxy-D-allose + NADP+
?
-
Substrates: 81% activity compared to 3,6-dideoxy-D-galactose
Products: -
Products: -
r
2-deoxy-D-ribose + NADP+
? + NADPH
-
Substrates: 18% of the activity compared to abequose
Products: -
Products: -
?
3,6-dideoxy-beta-D-galactofuranose + NADP+
3,6-dideoxy-D-galactono-1,4-lactone + NADPH
-
Substrates: i.e. abequose, furanose form, beta-configuration
Products: -
Products: -
?
3,6-dideoxy-D-galactose + NADP+
?
-
Substrates: 100% activity
Products: -
Products: -
r
3-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 36% of the activity compared to abequose
Products: -
Products: -
?
alpha-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 39% of the activity compared to alpha,beta-D-galactose and alpha,beta-L-arabinose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactose + NADP+
D-galatonolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
D-arabinose + NADP+
D-arabinolactone + NADPH
-
Substrates: 5% of the activity compared to abequose
Products: -
Products: -
?
D-fucose + NADP+
?
-
Substrates: 100% activity
Products: -
Products: -
?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH + H+
-
Substrates: 69% activity compared to D-fucose
Products: -
Products: -
?
L-arabinose + NAD+
L-arabino-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
?
-
Substrates: 12% activity compared to D-fucose
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinolactone + NADPH
-
Substrates: 6% of the compared to abequose
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 114% of the activity compared to abequose
Products: -
Products: -
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 90% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
2-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 90% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 94% of the activity compared to abequose
Products: -
Products: -
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 156% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
6-deoxy-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 156% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
alpha,beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
alpha,beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
Substrates: furanose form, beta-configuration
Products: -
Products: -
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactofuranose + NADP+
D-galactono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
Substrates: 63% of the activity compared to alpha,beta-L-arabinose and alpha,beta-D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
beta-L-arabinose + NADP+
L-arabinolactone + NADPH
-
Substrates: 63% of the activity compared to alpha,beta-L-arabinose and alpha,beta-D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: furanose form, beta-configuration
Products: gamma-lactone
Products: gamma-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabino-1,5-lactone + NADPH + H+
-
Substrates: 44% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
L-arabinose + NADP+
L-arabino-1,5-lactone + NADPH + H+
-
Substrates: 44% of the activity compared to D-galactose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
L-arabinose + NADP+
L-arabino-1,5-lactone + NADPH + H+
-
Substrates: 21% activity compared to D-fucose
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: 39% of the activity compared to alpha,beta-D-galactose and alpha,beta-L-arabinose
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
beta-D-galactose + NADP+
D-galatonolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: furanose form, beta-configuration
Products: gamma-lactone
Products: gamma-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: -
Products: product is assumed to be the corresponding -1,5-lactone
Products: product is assumed to be the corresponding -1,5-lactone
?
D-galactose + NADP+
D-galactonolactone + NADPH
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
complete inhibition at 1 mM, partial reversible by low concentration of cysteine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, ammonium sulfate precipitate, many months, without appreciable loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity increases at the beginning of salt stress, up to 3.6fold increase. Hypoosmotic stress does not induce the activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.120)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
