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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Pyrococcus woesei and UniProt Accession O52629

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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:
Pyrococcus woesei
UNIPROT: O52629
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The taxonomic range for the selected organisms is: Pyrococcus woesei
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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-
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beta-D-glactanase
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-
-
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beta-D-lactosidase
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-
-
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beta-galase
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-
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beta-lactosidase
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-
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driselase
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Exo-(1-->4)-beta-D-galactanase
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-
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exo-beta-(1->3)-D-galactanase
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galactosidase, beta
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Hydrolact
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lactase
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lactosylceramidase II
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Lactozym
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Maxilact
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-
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Oryzatym
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-
-
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p-nitrophenyl beta-galactosidase
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-
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S 2107
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-
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SR12 protein
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Sumiklat
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Trilactase
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-
-
-
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
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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-galactopyranose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
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-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
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-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
mutant YG6762
5.4 - 6.7
pH 5.4: about 90% of maximal activity, pH 6.7: about 40% of maximal activity
5.5
wild-type enzyme YH4502
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
93 - 110
93°C: maximal activity, 110°C: active at temperatures up to
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGAL_PYRWO
510
0
59057
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T29A/V213I/L217M/N277H/I387V/R491C/N496D
large range mutant screening after direct chemical evolution, the mutant variant YG6762 has nucleotide changes in 13 sites: T30C, A85G, C621A, G637A, T649A, A829V, T912G, C924T, A1159G, G1242C, C1471T, A1486G, and C1497A, the mutant YG6762 shows 4.9-7.5fold increased activity, dependent on the reaction temperature, but decreased thermostability, compared to the wild-type enzyme, overview, revertion of the mutation at each single of the 8 mutation sites results in decreased activity of the altered mutant, especially when reverting residue 277 to Asn, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
the mutant enzyme YG6762 shows 40% remaining activity after 1 h, and 30% remaining activity after 2 h, wild-type enzyme YH4502 shows over 75% remaining actiivty after 1 h, and more than 50% remiaing activity after 2 h
85
4 h, 11% loss of activity
93
4 h, 15% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene hlacz-sh, chemical synthesis of the gene derived from Pyrococcus woesei for direct evolution, DNA and amino acid sequence determination and anaylsis, library construction, expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta-Blue (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xiong, A.S.; Peng, R.H.; Zhuang, J.; Li, X.; Xue, Y.; Liu, J.G.; Gao, F.; Cai, B.; Chen, J.M.; Yao, Q.H.
Directed evolution of a beta-galactosidase from Pyrococcus woesei resulting in increased thermostable beta-glucuronidase activity
Appl. Microbiol. Biotechnol.
77
569-578
2007
Pyrococcus woesei (O52629), Pyrococcus woesei
Manually annotated by BRENDA team
Dabrowski, S.; Maciunska, J.; Synowiecki, J.
Cloning and nucleotide sequence of the thermostable beta-galactosidase gene from Pyrococcus woesei in Escherichia coli and some properties of the isolated enzyme
Mol. Biotechnol.
10
217-222
1998
Pyrococcus woesei (O52629), Pyrococcus woesei, Pyrococcus woesei DSM 3773 (O52629)
Manually annotated by BRENDA team