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Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession P22498
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EC Tree
3.2.1.23 beta-galactosidaseIUBMB 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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Word Map
- 3.2.1.23
- lacz
- adenovirus
- lysosomal
- lactose
- endothelial
- oligosaccharide
- artery
- phage
-
adenovirus-mediated
- beta-glucosidase
-
immunoassay
-
retroviral
- beta-glucuronidase
-
herpes
- lambda
- simplex
- luciferase
- cytomegalovirus
- neuraminidase
- viruses
- hydrolases
- bacteriophage
- glycosidases
- gm1
- liposome
- ganglioside
- p16ink4a
- alpha-galactosidase
- alpha-mannosidase
-
osteogenic
- vaccinia
-
adeno-associated
-
replication-defective
- n-acetyl-beta-glucosaminidase
- runx2
- sialidase
- alpha-glucosidase
-
sialic
-
galactosylation
-
plaque-forming
-
osteoblast
- kluyveromyces
- telomerase
- analysis
- degradation
- diagnostics
-
lysogens
- beta-hexosaminidase
- keratan
-
vector-mediated
- biotechnology
- molecular biology
- synthesis
- environmental protection
- ganciclovir
- nutrition
-
transglycosylation
- medicine
- industry
-
nonviral
- food industry
- biofuel production
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
beta-D-galactoside galactohydrolase
-
-
-
-
lactase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
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
9031-11-2
-
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-nitrophenyl beta-D-galactopyranose + H2O
2-nitrophenol + D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
the enzyme catalysed both hydrolysis and transglycosylation
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside + H2O
5-bromo-4-chloro-indol + beta-D-galactose
-
-
-
-
?
methyl-beta-D-galactopyranoside + H2O
methanol + beta-D-galactose
-
-
-
-
?
phenyl-beta-D-galactopyranoside + H2O
phenol + beta-D-galactose
-
-
-
-
?
additional information
?
-
quantitative determination of the products of the transglycosylation reactions shows that the amount of glucose is always much higher than that of galactose, which indicates that, during the reaction, galactoside of lactose is used in the transglycosylation reaction to form galactooligosaccharides. Compared to the wild-type enzyme, the yields of galacto-oligosaccharides produced by F441Y and F359Q are increased by 10.8% and 7.4%, respectively
-
-
?
additional information
?
-
the enzyme catalyzes the production of the synthetic disaccharide lactulose (4-O-beta-D-galactopyranosyl-D-fructose) via a transgalactosylation using lactose as a galactose donor and fructose as an acceptor
-
-
?
additional information
?
-
-
the enzyme displays a quite broad specificity, showing wide tolerance regarding the structure of the aglycon moiety, overview
-
-
?
additional information
?
-
-
the recombinant enzyme produces galactooligosaccharides from lactose by transgalactosylation. Galactooligosaccharide production increases with increasing lactose concentration, whereas the yield of galactooligosaccharides from lactose is almost constant. The final concentration of galactooligosaccharide is maximal at 80°C
-
-
?
additional information
?
-
-
the selectivity hexanol vs. water increases with increasing water activity in the reaction medium. It seems that the ideal condition for the transglycosylation reaction is a water activity close to 1.0
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-aminophenyl beta-D-thiogalactopyranoside
-
competitive inhibition
additional information
-
no inhibition by 4-chloromercuribenzoate or N-ethylmaleimide, and by D-galactose and isopropyl beta-D-thiogalactopyranoside
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics and thermodynamics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
186
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme delVal484-His489
219
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme His489
309
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
310
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
416
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R489A
435
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
450
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R488A
498
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
160
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
251
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
382
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
584
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, wild-type enzyme
698
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, recombinant enzyme
772
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, wild-type enzyme
7
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
217
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
234
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
299
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
132
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
830
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
1004
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, recombinant enzyme
1084
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, wild-type enzyme
1446
4-nitrophenyl cellobioside
-
pH 6.5, 75°C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
152.3
pH 7.5, 80°C, activity of recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl beta-D-galactopyranoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl beta-D-galactopyranoside
6.5
additional information
-
transgalactosylation activity is optimal at pH 6.0
6
substrate: 2-nitrophenyl beta-D-galactopyranoside, mutant enzymes F441Y and F359Q
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
pH 4.0: about 45% of maximal activity, pH 8.0: about 80% of maximal activity
4.5 - 7.5
pH 4.5: about 85% of maximal activity, pH 7.5: about 50% of maximal activity, recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl-beta-D-galactopyranoside
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
90
substrate: 2-nitrophenyl beta-D-galactopyranoside, at pH 6.5, wild-type enzyme
85
substrate: 2-nitrophenyl beta-D-galactopyranoside, at pH 6.5, mutant enzymes F441Y and F359Q
85
recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl beta-D-galactopyranoside
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
65°C; about 55% of maximal activity, 95°C: about 90% of maximal activity, recombinant mutant enzyme F441Y, substrate: 2-nitrophenyl-beta-D-galactopyranoside
70 - 95
70°C: about 60% of maximal activity, 95°C: about 70% of maximal activity
80 - 90
substrate: 2-nitrophenyl beta-D-galactopyranoside, mutant enzymes F441Y and F359Q show 80% of their maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism, is complemented with one of the missing proteins, the beta-galactosidase (SSO3019). The beta-galactosidase complemented strain shows reduced carbohydrate content of the isolated total extracellular polymeric substance implying a role in the modulation of the produced EPS during static biofilm formation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F359Q
compared to wild-type enzyme the mutant enzyme is less stable at 75°C, the optimum is similar to that of wild-type enzyme. Km of the mutant enzyme is increased about 2fold and the kcat is increased by 32.3%
F441Y
additional information
-
isolation of three phenotypically stable mutants by screening on activity against 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside, isolation of the insertion sequence ISC1217 from the mutant enzymes, ISC1217 contains terminal inverted repeats and is flanked by a direct repeat of 6 bp, overview
F441Y
compared to wild-type enzyme the mutant enzyme is less stable at 75°C, the optimum is similar to that of wild-type enzyme. Km of the mutant enzyme is increased about 2fold and the kcat is increased by 36.6%
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
80
85
100
-
purified enzyme, pH 6.5, complete loss of activity after 15 min
70
-
half-life: 720 h, thermal deactivation of galactooligosaccharide production
75
80
85
90
-
half-life: 9.3 h, thermal deactivation of galactooligosaccharide production
95
-
purified enzyme, pH 6.5, complete loss of activity after 120 min
75
half-life of mutant enzyme F441Y is 75 h, half-life of mutant enzyme F359Q is 85 h. Activity of wild-type enzyme increases slowly within the first 45 h, it retains 90% of its initial activity after incubation for approximately 80 h. After 80 h, the activity decreases rapidly
75
50% loss of activity after 12 h, recombinant mutant enzyme F441Y
80
50% loss of activity after 11 h, recombinant mutant enzyme F441Y
85
50% loss of activity after 5.5 h, recombinant mutant enzyme F441Y
75
-
half-life: 208 h, thermal deactivation of galactooligosaccharide production
80
-
half-life: 77 h, thermal deactivation of galactooligosaccharide production
85
-
half-life: 42 h, thermal deactivation of galactooligosaccharide production
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 50 mM sodium phosphate, pH 6.5, and 2.8 mM 4-nitrophenyl-beta-D-galactopyranoside, stable for long periods of storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble enzyme partially from Saccharomyces cerevisiae by heat treatment at 75°C for 30 min, and ultrafiltration
-
soluble, native enzyme 966fold by anion exchange chromatography, precipitation at pH 4.5, dialysis, 4-aminophenyl-beta-D-thiogalactopyranoside affinity chromatography, and another step of anion exchange chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a soluble protein that contained a hexa-histidine tag at the carboxyl terminus
expression in simian CV1 and murine NIH3T3 cell lines. The recombinant protein has no cytotoxic effect on the host cells
overexpression in Sulfolobus solfataricus mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli, enzyme activity is only detected when translation is initiated at the ATG at position 118
-
gene lacS, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
gene lacS, expression in Saccharomyces cerevisiae strain ScKY117 using a galactose-inducible promoter, the strong, heat-inducible upstream activating RcC9 sequence of the yeast genes GAL1 and GAL10, originally isolated from Caenorhabditis elegans, transcription of the lacS gene under the control of this sequence is rapidly and efficiently induced by heat shock, the recombinant enzyme is identical in molecular mass, thermostability, and thermophilicity to the native enzyme, heat induction by growth at 39°C for 45 min, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme catalyzes the production of the synthetic disaccharide lactulose (4-O-beta-D-galactopyranosyl-D-fructose) via a transgalactosylation using lactose as a galactose donor and fructose as an acceptor. Lactulose is used in treatment of hyperammonemia and as a gentle laxative. It is also applied to commercial infant formulas and various milk products because it specifically promotes the intestinal proliferation of Bifidobacterium, which creates an acid medium that inhibits the growth of undesirable bacteria
synthesis
the F441Y mutant enzyme has potential application in the industrial preparation of galactooligosaccharides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pearl, L.H.; Hemmings, A.M.; Nucci, R.; Rossi, M.
Crystallization and preliminary X-ray analysis of the beta-galactosidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
J. Mol. Biol.
229
561-563
1993
Saccharolobus solfataricus
Pisani, F.M.; Rella, R.; Raia, C.A.; Rozzo, C.; Nucci, R.; Gambacorta, A.; De Rosa, M.; Rossi, M.
Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties
Eur. J. Biochem.
187
321-328
1990
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
Moracci, M.; La Volpe, A.; Pulitzer, J.F.; Rossi, M.; Ciaramella, M.
Expression of the thermostable beta-galactosidase gene from the archaebacterium Sulfolobus solfataricus in Saccharomyces cerevisiae and characterization of a new inducible promoter for heterologous expression.
J. Bacteriol.
174
873-882
1992
Saccharolobus solfataricus
Schleper, C.; Rder, R.; Singer, T.; Zillig, W.
An insertion element of the extremely thermophilic archaeon Sulfolobus solfataricus transposes into the endogenous beta-galactosidase gene
Mol. Gen. Genet.
243
91-96
1994
Saccharolobus solfataricus
Little, S.; Cartwright, P.; Campbell, C.; Prenneta, A.; McChesney, J.; Mountain, A.; Robinson, M.
Nucleotide sequence of a thermostable beta-galactosidase from Sulfolobus solfataricus
Nucleic Acids Res.
17
7980
1989
Saccharolobus solfataricus
Park, A.R.; Oh, D.K.
Galacto-oligosaccharide production using microbial beta-galactosidase: current state and perspectives
Appl. Microbiol. Biotechnol.
85
1279-1286
2010
Alicyclobacillus acidocaldarius, Aspergillus aculeatus, Aspergillus oryzae, Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Bifidobacterium adolescentis, Bifidobacterium bifidum, Bifidobacterium longum subsp. infantis, Caldicellulosiruptor saccharolyticus, Kluyveromyces marxianus, Papiliotrema laurentii, Streptococcus pneumoniae, Pantoea agglomerans, Kluyveromyces lactis, Lactobacillus acidophilus, Limosilactobacillus reuteri, Saccharopolyspora rectivirgula, Hamamotoa singularis, Sterigmatomyces elviae, Saccharolobus solfataricus, Thermotoga maritima, Thermus aquaticus, Thermus sp., Arthrobacter psychrolactophilus
Kim, Y.-S.; Park, C.-S.; Oh, D.-K.
Lactulose production from lactose and fructose by a thermostable beta-galactosidase from Sulfolobus solfataricus
Enzyme Microb. Technol.
39
903-908
2006
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
-
Wu, Y.; Yuan, S.; Chen, S.; Wu, D.; Chen, J.; Wu, J.
Enhancing the production of galacto-oligosaccharides by mutagenesis of Sulfolobus solfataricus beta-galactosidase
Food Chem.
138
1588-1595
2013
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
Cannio, R.; de Pascale, D.; Rossi, M.; Bartolucci, S.
Gene expression of a thermostable beta-galactosidase in mammalian cells and its application in assays of eukaryotic promoter activity
Biotechnol. Appl. Biochem.
19
233-244
1994
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
Hansson, T.; Andersson, M.; Wehtje, E.; Adlercreutz, P.
Influence of water activity on the competition between beta-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol
Enzyme Microb. Technol.
29
527-534
2001
Escherichia coli, Saccharolobus solfataricus
-
Koerdt, A.; Jachlewski, S.; Ghosh, A.; Wingender, J.; Siebers, B.; Albers, S.V.
Complementation of Sulfolobus solfataricus PBL2025 with an alpha-mannosidase: effects on surface attachment and biofilm formation
Extremophiles
16
115-125
2012
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
Cubellis, M.V.; Rozzo, C.; Montecucchi, P.; Rossi, M.
Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene
Gene
94
89-94
1990
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
Sun, X.; Duan, X.; Wu, D.; Chen, J.; Wu, J.
Characterization of Sulfolobus solfataricus beta-galactosidase mutant F441Y expressed in Pichia pastoris
J. Sci. Food Agric.
94
1359-1365
2014
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
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