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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Arthrobacter sp. SB and UniProt Accession Q7WTU5

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EC Tree
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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This record set is specific for:
Arthrobacter sp. SB
UNIPROT: Q7WTU5
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Word Map
The taxonomic range for the selected organisms is: Arthrobacter sp. SB
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
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-
-
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beta-D-galactoside galactohydrolase
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-
-
-
beta-D-glactanase
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-
-
-
beta-D-lactosidase
-
-
-
-
beta-galase
-
-
-
-
beta-lactosidase
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-
-
-
BgaS
-
-
-
driselase
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-
-
-
Exo-(1-->4)-beta-D-galactanase
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-
-
-
exo-beta-(1->3)-D-galactanase
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-
-
-
galactosidase, beta
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-
-
-
Hydrolact
-
-
-
-
lactase
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-
-
-
lactosylceramidase II
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-
-
-
Lactozym
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-
-
-
Maxilact
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-
-
-
Oryzatym
-
-
-
-
p-nitrophenyl beta-galactosidase
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-
-
-
S 2107
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-
-
-
SR12 protein
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-
-
-
Sumiklat
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-
-
-
Trilactase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
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
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O
5-bromo-4-chloroindol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
additional information
?
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-
substrate specificity of recombinant wild-type and mutant enzymes, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7WTU5_9MICC
1053
0
113737
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
three-dimensional structure modeling of BgaS, homotetramer that forms a diamond shape with two axes: a long interface and an activating interface, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E229D
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site-directed mutagenesis, enzyme BgaS7a, the mutant shows slightly increased activity compared to the wild-type enzyme
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E229D/G803D
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site-directed mutagenesis, inactive mutant
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G803D
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site-directed mutagenesis, inactive mutant
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V405A/G803D
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site-directed mutagenesis, inactive mutant
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additional information
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gene bgaS3 encoding a loss of function variant is subjected to random mutagenesis to restore activity and discover potential interactions important in cold activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coker, J.A.; Brenchley, J.E.
Protein engineering of a cold-active beta-galactosidase from Arthrobacter sp. SB to increase lactose hydrolysis reveals new sites affecting low temperature activity
Extremophiles
10
515-524
2006
Arthrobacter sp., Arthrobacter sp. SB
Manually annotated by BRENDA team