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Ba2+
-
1 mM, minor stimulation
Cr3+
115.0% relative activity at 2 mM
Hg2+
110.4% relative activity at 2 mM
Pb2+
105.6% relative activity at 2 mM
Al3+
-
0.1 mM, activation to 118% of initial activity
Al3+
-
1 mM, 30% activation
Ca2+
-
2.5 mM CaCl2, activates hydrolysis of lactose and p-nitrophenyl-beta-D-galactoside
Ca2+
108.7% relative activity at 10 mM
Ca2+
-
0.01 mM, activation at low concentrations in a system containing Na+ at optimal concentration
Ca2+
-
activates at 50-100 mg/l, inhibits at concentrations above 200 mg/l
Ca2+
-
0.32 mM, activates isoenzyme betaG550
Ca2+
-
1 mM, 1.85fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside
Ca2+
-
1 mM, minor stimulation
Ca2+
-
0.01 mM, activates
Ca2+
-
slightly stimulates activity
Co2+
109.1% relative activity at 10 mM
Co2+
-
0.1 mM, activation in a system containing Na+ at optimal concentration
Co2+
-
1 mM, 8.1fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 4.7fold stimulation of activity with lactose
Co2+
-
0.1 mM, activation to 124% of initial activity
Co2+
the enzyme requires 1 mM Co2+ for optimal activity and thermostability
Co2+
Saccharomyces fragilis
-
-
Co2+
Saccharomyces fragilis
-
maximal activation at 0.1 mM
Co2+
-
30 mM, 6% activation
Cu2+
110.1% relative activity at 10 mM
Fe2+
-
0.01-0.1 mM, activation in a system containing Na+ at optimal concentration
Fe2+
-
activates at 50-100 mg/l, inhibits at concentrations above 200 mg/l
Fe2+
-
1 mM, 4.5fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 4.1fold stimulation of activity with lactose
Fe3+
104.4.4% relative activity at 10 mM
K+
slight stimulation
K+
-
49% increase of activity at 5 mM
K+
activates enzymatic activity
K+
107.7% relative activity at 10 mM
K+
-
activates hydrolysis of p-nitrophenyl-beta-D-galactoside and p-nitrophenyl alpha-L-arabinoside more effectively than Na+
K+
-
activates hydrolysis of lactose more effectively than Na+
K+
-
0.32 mM KCl, activates isoenzyme betaG550
K+
-
326% relative activity at 10 mM
K+
-
10 mM, slight activation
K+
-
either 10 mM K+ or 10 mM Na+ is required for maximal activity, strain L103
K+
-
either 10 mM K+ or 10 mM Na+ is required for maximal activity, strain L461
K+
-
maximal activation of cell wall enzyme and extracellular enzyme by Na+ and Zn2+
K+
Saccharomyces fragilis
-
-
K+
Saccharomyces fragilis
-
activates
K+
-
synergistic activation with Mg2+ and Na+ or Mg2+ and K+. Na+ is the better activator with either o-nitrophenyl-D-galactoside or 4-methylumbelliferyl-beta-D-galactoside as substrates while K+ is the better activator of lactose and p-nitrophenyl-beta-D-galactoside
K+
-
slightly stimulates activity
KCl
the activity of the enzyme in 2.5 M and 4 M KCl relative to 4 M NaCl is 34% and 40%, respectively
KCl
maximal activity in either 4 M NaCl or KCl
KCl
requires 4-4.5 M NaCl or KCl for maximal activity
KCl
still active in presence of 4 M, more active in presence of KCl than in presence of NaCl
Li+
110.1% relative activity at 10 mM
Li+
-
50 mM, minor stimulation
Mg2+
stimulation
Mg2+
-
the enzyme requires metal ions, Mg2+ or Mn2+ can restore the enzyme activity of recombinant wild-type and mutant apoenzymes, but not Ca2+, Cu2+, and Na+, overview
Mg2+
-
activation of the recombinant hybrid enzyme
Mg2+
Bacteroides polypragmatus
-
required, optimal concentration 5-10 mM
Mg2+
-
stimulates activity
Mg2+
-
strain ML 308 shows absolute requirement, strain ML 309 does not
Mg2+
-
0.1-10 mM, activation in a system containing Na+ at optimal concentration
Mg2+
-
activates at 50-200 mg/l
Mg2+
beta-galactosidase requires Mg2+ for full catalytic activity, one Mg2+ is at each active site but 3-4 others bind to other parts of each subunit
Mg2+
the active site of beta-galactosidase contains a Mg2+ ion ligated by Glu-416, His-418 and Glu-461 plus three water molecules
Mg2+
-
0.32 mM MgCl2, activates isoenzyme betaG550 and betaG19
Mg2+
-
1 mM, 7fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 5.4fold stimulation of activity with lactose
Mg2+
-
activation of both the wild-type Kluyveromyces lactis enzyme and the recombinant hybrid enzyme
Mg2+
-
enhances activity and stability
Mg2+
-
the enzyme needs MgCl2 for its stability retaining 73% and 85% of its activity after an incubation at 37°C for 5 h in the presence of 1 and 10 mM MgCl2, 414% relative activity at 10 mM
Mg2+
activates 21-28% at 1-10 mM
Mg2+
the enzyme requires 1 mM Mn2+ for optimal activity and thermostability
Mg2+
-
10 mM MgCl2, 3fold higher activity
Mg2+
-
maximal activation of intracellular enzyme by Mg2+ or Mn2+
Mg2+
5 mM, 1.1fold stimulation of activity, 80°C, pH 7.0
Mg2+
Saccharomyces fragilis
-
-
Mg2+
Saccharomyces fragilis
-
maximal activation at 1 mM
Mg2+
-
0.01 mM, activates
Mg2+
-
30 mM, 20% activation
Mg2+
-
enhances stability
Mg2+
-
synergistic activation with Mg2+ and Na+ or Mg2+ and K+. Na+ is the better activator with either o-nitrophenyl-D-galactoside or 4-methylumbelliferyl-beta-D-galactoside as substrates while K+ is the better activator of lactose and p-nitrophenyl-beta-D-galactoside
Mg2+
-
contains 0.19 Mg2+ per monomer
Mn2+
slight stimulation
Mn2+
-
the enzyme requires metal ions, Mg2+ or Mn2+ can restore the enzyme activity of recombinant wild-type and mutant apoenzymes, but not Ca2+, Cu2+, and Na+, overview
Mn2+
-
11% increase of activity at 5 mM
Mn2+
activates enzymatic activity
Mn2+
-
activates the recombinant hybrid enzyme
Mn2+
-
2.5 mM MnCl2, activates hydrolysis of lactose and p-nitrophenyl-beta-D-galactoside
Mn2+
-
0.01-0.1 mM, activation in a system containing Na+ at optimal concentration
Mn2+
-
1 mM, 8.9fold stimulation of activity with o-nitrophenyl beta-D-galactopyranoside, 5.6fold stimulation of activity with lactose
Mn2+
-
activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme
Mn2+
-
0.2 mM, slight activation
Mn2+
-
0.1 mM, activation to 120% of initial activity
Mn2+
-
341% relative activity at 10 mM
Mn2+
-
10 mM, slight activation
Mn2+
-
0.0274% of Mn2+ ions lead to 18% enhancement of beta-galactosidase activity in strain CF2-7F
Mn2+
-
maximal activation of intracellular enzyme by Mg2+ or Mn2+
Mn2+
-
1 mM, minor stimulation
Mn2+
Saccharomyces fragilis
-
-
Mn2+
Saccharomyces fragilis
-
maximal activation at 0.1 mM
Mn2+
-
0.01 mM, activates
Mn2+
-
30 mM, 25% activation
Mn2+
-
10 mM MnCl2, 2fold activation
Mn2+
-
enhances stability
Mn2+
-
most effective divalent cation for beta-galactosidase activity on both o-nitrophenyl-beta-D-galactoside and lactose
Mn2+
Torulopsis sphaerica
-
0.2 mM, slight activation
Mn2+
-
0.2 mM, slight activation
Na+
-
53% increase of activity at 5 mM
Na+
activates enzymatic activity
Na+
105.3% relative activity at 2 mM
Na+
-
activates hydrolysis of o-nitrophenyl-beta-D-galactoside more effectively than K+
Na+
the active site of beta-galactosidase contains a Na+ ion
Na+
-
hydrolysis of 4-methylumbelliferyl-beta-D-galactoside is mildly stimulated by NaCl
Na+
-
0.32 mM NaCl or NaF, activates isoenzyme betaG550
Na+
-
165% relative activity at 10 mM
Na+
-
either 10 mM K+ or 10 mM Na+ is required for maximal activity, strain L103
Na+
-
either 10 mM K+ or 10 mM Na+ is required for maximal activity, strain L461
Na+
-
50 mM, minor stimulation
Na+
-
half-maximal activation at 0.1 mM
Na+
-
synergistic activation with Mg2+ and Na+ or Mg2+ and K+. Na+ is the better activator with either o-nitrophenyl-D-galactoside or 4-methylumbelliferyl-beta-D-galactoside as substrates while K+ is the better activator of lactose and p-nitrophenyl-beta-D-galactoside
Na+
-
slightly stimulates activity
NaCl
optimally active at 4 M NaCl
NaCl
maximal activity in either 4 M NaCl or KCl
NaCl
requires 4-4.5 M NaCl or KCl for maximal activity
NaCl
still active in presence of 4 M, more active in presence of KCl than in presence of NaCl
Ni2+
-
activates the recombinant hybrid enzyme
Ni2+
103.4% relative activity at 2 mM
Ni2+
-
0.1 mM, activation in a system containing Na+ at optimal concentration
Ni2+
-
activates the recombinant hybrid enzyme, but inhibits the wild-type Kluyveromyces lactis enzyme
Ni2+
-
0.1 mM, activation to 118% of initial activity
Sn2+
-
2.5 mM SnCl2, activates hydrolysis of lactose
Zn2+
105.2% relative activity at 10 mM
Zn2+
-
0.01-0.1 mM, activation in a system containing Na+ at optimal concentration
Zn2+
-
slightly activates the wild-type Kluyveromyces lactis enzyme, but slightly inhibits the recombinant hybrid enzyme
Zn2+
-
maximal activation of cell wall enzyme and extracellular enzyme by Na+ and Zn2+
Zn2+
-
30 mM, 10% activation
additional information
the enzyme is not affected by 5 mM of Mg2+, Mn2+, or Ca2+
additional information
-
the enzyme is not affected by 5 mM of Mg2+, Mn2+, or Ca2+
additional information
-
the enzyme is not affected by Mg2+
additional information
the activity is not considerably affected by Na+, K+, Mg2+, Co2+, and Ca2+ (5 mM)
additional information
-
the activity is not considerably affected by Na+, K+, Mg2+, Co2+, and Ca2+ (5 mM)
additional information
not stimulated by Mg2+ and Mn2+
additional information
-
the addition of Mg2+ does not cause significant change in the activity of beta-galactosidase in all the tested strains except in MF14C
additional information
-
purified enzyme does not require Ca2+, Cu2+, Zn2+ or Mg2+