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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Oryza sativa and UniProt Accession Q10RB4

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IUBMB Comments
Some enzymes in this group hydrolyse alpha-L-arabinosides; some animal enzymes also hydrolyse beta-D-fucosides and beta-D-glucosides; cf. EC 3.2.1.108 lactase.
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Select one or more organisms in this record: ?
This record set is specific for:
Oryza sativa
UNIPROT: Q10RB4
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The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-galactosidase, beta-gal, beta-d-galactosidase, senescence-associated beta-galactosidase, endo-beta-galactosidase, bglap, sa-beta-gal, acid beta-galactosidase, beta galactosidase, betagal, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid beta-galactosidase
-
-
-
-
beta-D-galactoside galactohydrolase
-
-
-
-
beta-D-glactanase
-
-
-
-
beta-D-lactosidase
-
-
-
-
beta-galase
-
-
-
-
beta-lactosidase
-
-
-
-
driselase
-
-
-
-
Exo-(1-->4)-beta-D-galactanase
-
-
-
-
exo-beta-(1->3)-D-galactanase
-
-
-
-
galactosidase, beta
-
-
-
-
Hydrolact
-
-
-
-
lactase
-
-
-
-
lactosylceramidase II
-
-
-
-
Lactozym
-
-
-
-
Maxilact
-
-
-
-
Oryzatym
-
-
-
-
p-nitrophenyl beta-galactosidase
-
-
-
-
S 2107
-
-
-
-
SR12 protein
-
-
-
-
Sumiklat
-
-
-
-
Trilactase
-
-
-
-
additional information
cf. EC 3.2.1.145
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-galactoside galactohydrolase
Some enzymes in this group hydrolyse alpha-L-arabinosides; some animal enzymes also hydrolyse beta-D-fucosides and beta-D-glucosides; cf. EC 3.2.1.108 lactase.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-11-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
ir
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
ir
galactoxyloglucan + H2O
galactose + ?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
pectic galactan + H2O
galactose + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
the OsBGal1 isozyme releases significant amounts of galactose from 1,3-, 1,4-, and 1,6-beta-linked galactose di- and trisaccharides, with beta-1,3-galactobiose and beta-1,3-galactotriose appearing to be hydrolyzed the fastest, no activity of isozyme OsBGal1 with lactose, as well as with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-mannoside, 4-nitrophenyl-beta-D-arabinoside, and 4-nitrophenyl-beta-D-xyloside
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
complete inhibition at 10 mM of recombinant isozyme OsGal1
D-galactose
10% inhibition at 5 mM of recombinant isozyme OsGal1
D-gluconolactone
40% inhibition at 10 mM of recombinant isozyme OsGal1
delta-galactonolactone
62% inhibition at 10 mM of recombinant isozyme OsGal1
Fe3+
complete inhibition at 1 mM of recombinant isozyme OsGal1
Hg2+
complete inhibition at 1 mM of recombinant isozyme OsGal1
IPTG
38% inhibition at 10 mM of recombinant isozyme OsGal1
lactose
15% inhibition at 5 mM of recombinant isozyme OsGal1
Mg2+
27% inhibition at 10 mM of recombinant isozyme OsGal1
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
40% activation at 10 mM of recombinant isozyme OsGal1
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
4-nitrophenyl-beta-D-galactopyranoside
pH 3.5, 60°C, recombinant isozyme OsGal1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
recombinant isozyme BGal1 in Escherichia coli, substrate 4-nitrophenyl-beta-D-galactopyranoside
0.04
recombinant isozyme BGal2 in Escherichia coli, substrate 2-nitrophenyl-beta-D-galactopyranoside
0.058
recombinant isozyme BGal1 in Escherichia coli, substrate 2-nitrophenyl-beta-D-galactopyranoside
0.083
recombinant isozyme BGal2 in Escherichia coli, substrate 4-nitrophenyl-beta-D-galactopyranoside
65.1
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.5
recombinnat isozyme OsGal1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 5
inactivation at pH 2.5, half-maximal activity at pH 4.5-5.0, recombinant isozyme OsGal1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
recombinant isozyme OsGal1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
precursor; two isozymes OsBGal1 and OsBGal2
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
germinating rice, enzyme location in the embryo, aleurone layer and surrounding tissues, and in the radicle and shoot after germination
Manually annotated by BRENDA team
additional information
developmental distribution of isozyme expression in rice tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97000
x * 97000, isozyme OsGal1, SDS-PAGE
40000
-
1 * 47000 + 1 * 40000, SDS-PAGE
47000
-
1 * 47000 + 1 * 40000, SDS-PAGE
65000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 97000, isozyme OsGal1, SDS-PAGE
dimer
-
1 * 47000 + 1 * 40000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
30°C, 60 min, slow inactivation above
655054
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
10 min, purified recombinant isozyme OsGal1, rapid inactivation above
45
-
pH 4.0, 60 min, inactivation above
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant OsBGal1 thioredoxin fusion protein 23fold from Escherichia coli by nickel affinity and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes OsBGal1 and OsBGal2, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression of soluble isozymes in Escherichia coli, expression of isozyme OsBGal1 thioredoxin fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaneko, S.; Kobayashi, H.
Purification and characterization of extracellular beta-galactosidase secreted by supension cultured rice (Oryza sativa L.) cells
Biosci. Biotechnol. Biochem.
67
627-630
2003
Oryza sativa
Manually annotated by BRENDA team
Chantarangsee, M.; Tanthanuch, W.; Fujimura, T.; Fry, S.C.; Ketudat Cairns, J.
Molecular characterization of ?-galactosidases from germinating rice (Oryza sativa)
Plant Sci.
173
118-134
2007
Oryza sativa (Q10RB4)
Manually annotated by BRENDA team