Any feedback?
Information on EC 3.2.1.23 - beta-galactosidase and Organism(s) Lactobacillus delbrueckii and UniProt Accession Q1G9Z4
for references in articles please use BRENDA:EC3.2.1.23Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
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: Lactobacillus delbrueckii
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
-
-
-
-
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-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
?
o-nitrophenyl-beta-D-galactoside + H2O
o-nitrophenol + beta-D-galactose
-
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
the enzyme is involved in lactose fermentation in the colon playing a central role in lactose intolerance in humans
-
-
?
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
lactose + H2O
D-glucose + D-galactose
-
the enzyme is involved in lactose fermentation in the colon playing a central role in lactose intolerance in humans
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
the enzyme requires 1 mM Co2+ for optimal activity and thermostability
Mg2+
the enzyme requires 1 mM Mn2+ for optimal activity and thermostability
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not significantly inhibited by Fe2+, Ca2+, Mg2+, Zn2+, Ba2+, and Ni2+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
0.17
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
0.94
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
0.98
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
0.365
o-nitrophenyl-beta-D-galactoside
-
wild-type enzyme, at 11-45°C
0.371
o-nitrophenyl-beta-D-galactoside
-
mutant enzyme L317F, 11-45°C
0.479
o-nitrophenyl-beta-D-galactoside
-
mutant enzyme P429S, at 11-45°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
47.2
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
49.2
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
45.7
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
46.3
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
289.4
2-nitrophenyl-beta-D-galactopyranoside
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
295
2-nitrophenyl-beta-D-galactopyranoside
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
46.6
lactose
wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C
47
lactose
mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 11842, subspecies Lactobacillus delbrueckii bulgaricus
UniProt
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
2 * 110000, wild-type enzyme and mutant enzymes L317D and P429S, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 110000, wild-type enzyme and mutant enzymes L317D and P429S, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E491A
the mutant shows wild type optimal temperature, but displays an optimal pH at 6.5-7.0
L317F
-
maximal velocity deviates from that of wild-type enzyme only at lower temperatures, in 2 mM Mg2+. This temperature-dependent effect can be suppressed by increasing the Mg2+ concentration
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
the wild type protein retains about 90% of its activity after 32 h at pH 5.5. At pH 5.0 and 6.0 the enzyme conserves more than 50% of its initial activity after 32 h of incubation, at pH 4.5, 6.5, 7.0 and 7.5 the enzyme half-lives are 24, 28, 20 and 18 h respectively
706705
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 65
the wild-type beta-galactosidase is fully stable at 40°C and 45°C for 16 h, respectively. At temperatures of 50, 55, 60 and 65°C wild type enzyme half-lives are 6, 3, 1.5 and 0.4 h respectively. Above 65°C occurs rapid inactivation with or without divalent ions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and fast-performance liquid chromatography using an anion-exchange column equilibrated with 100 mM sodium acetate buffer (pH 5.5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
the enzyme is used for hydrolysis of lactose extracted from whey or milk
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adams, R.M.; Yoast, S.; Mainzer, S.E.; Moon, K.; Palombella, A.L.; Estell, D.A.; Power, S.D.; Schmidt, B.F.
Characterization of two cold-sensitive mutants of the beta-galactosidase from Lactobacillus delbruckii subsp. Bulgaricus
J. Biol. Chem.
8
5666-5672
1994
Lactobacillus delbrueckii
Honda, H.; Kataoka, F.; Nagaoka, S.; Kawai, Y.; Kitazawa, H.; Itoh, H.; Kimura, K.; Taketomo, N.; Yamazaki, Y.; Tateno, Y.; Saito, T.
beta-Galactosidase, phospho-beta-galactosidase and phospho-beta-glucosidase activities in Lactobacilli strains isolated from human faeces
Lett. Appl. Microbiol.
45
461-466
2007
Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lacticaseibacillus casei, Limosilactobacillus fermentum, Lactobacillus crispatus, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. lactis, Lactobacillus johnsonii, Limosilactobacillus reuteri, Ligilactobacillus salivarius, Lactobacillus amylovorus, Limosilactobacillus mucosae, no activity in Lactobacillus gasseri, Limosilactobacillus oris, Limosilactobacillus vaginalis, Limosilactobacillus vaginalis MEP181R91, Limosilactobacillus reuteri MEP181R88
Rhimi, M.; Aghajari, N.; Jaouadi, B.; Juy, M.; Boudebbouze, S.; Maguin, E.; Haser, R.; Bejar, S.
Exploring the acidotolerance of beta-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus: an attractive enzyme for lactose bioconversion
Res. Microbiol.
160
775-784
2009
Lactobacillus delbrueckii (Q1G9Z4)
EXTERNAL LINKS (specific for EC-Number 3.2.1.23)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
