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Li+
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
Na+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like Na+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
Rhodopseudomonas rubrum
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
less effective than Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Ca2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
the enzyme is slightly activated by Ca2+ (85% relative activity at 5 mM)
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
less effective than Mg2+
Ca2+
-
binding of substrates also takes place in the absence of metal ions
Ca2+
-
in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Ca2+
-
requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Ca2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Ca2+
-
residual activity even in the presence of EDTA
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
Megalodesulfovibrio gigas
-
-
Co2+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Co2+
Co2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
about 50% as effective as Mg2+
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
about 50% as effective as Mg2+
Cobalt
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Cobalt
Megalodesulfovibrio gigas
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Fe2+
-
slight activation
Fe2+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Fe2+
Fe2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Fe2+
Rhodopseudomonas rubrum
-
slight activation
K+
the enzyme is highly activated by K+, the optimal concentration is 10 mM
K+
150 mM, optimal concentration
K+
maximum stimulation at 100 mM
K+
maximum stimulation at 100 mM
K+
maximum stimulation at 400 mM
K+
maximum stimulation at 200 mM
K+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like K+
K+
XP_019937160.1
100 mM, optimal concentration
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
-
MgADP- is true substrate
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
the enzyme activity is highly dependent on Mg2+, and the optimal concentration of Mg2+ is 2 mM
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
direct Mg2+ binding activates adenylate kinase from Escherichia coli in addition to ATP-complexed Mg2+, Mg2+ can bind to adenylate kinase directly prior to AMP binding
Mg2+
-
MgATP2- is true substrate
Mg2+
-
MgADP- is true substrate
Mg2+
-
MgATP2- is true substrate
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
Megalodesulfovibrio gigas
required for activity
Mg2+
activity is Mg2+ dependent
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mg2+
-
MgATP2- is true substrate
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
the adenylate kinase-catalyzed reaction requires a nucleotide complexed with Mg2+ as one substrate and a free nucleotide as the second substrate, maximum enzyme activity when [Mg2+]/[ATP] equals 1
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
-
MgADP- is true substrate
Mg2+
Rhodopseudomonas rubrum
-
requirement
Mg2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
Rhodopseudomonas rubrum
-
MgADP- is true substrate
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mg2+
-
MgATP2- is true substrate
Mg2+
-
binding of substrates also takes place in the absence of metal ions
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mg2+
-
MgADP- is true substrate
Mg2+
-
inhibits at high concentrations
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
no absolute requirement: 20% of activity in its absence
Mg2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Mg2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Mg2+
-
residual activity even in the presence of EDTA
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgADP- is true substrate
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
requirement, about 50% as effective as Mg2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
binding of substrates also takes place in the absence of metal ions
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mn2+
-
requirement, about 25% as effective as Mg2+
Mn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Mn2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Mn2+
-
residual activity even in the presence of EDTA
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
requirement, about 50% as effective as Mg2+
NH4+
the enzyme is highly activated by NH4+ (93.6% relative activity at 5 mM)
NH4+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like NH4+
Zinc
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Zinc
Megalodesulfovibrio gigas
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Zn2+
-
0.8-1 mol Zn2+ for wild-type and mutants H138N, D153C and D153T, 0.6 mol Zn2+ for mutant D153T, or 0.34 mol Zn2+ for mutant C130H per mol protein, atomic absorption spectrophotometry
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
1 mol per mol of enzyme, residual activity after loss
Zn2+
-
requirement, tightly bound, 0.8 mol Zn2+ per mol protein, atomic absorption spectrophotometry
Zn2+
Megalodesulfovibrio gigas
-
-
Zn2+
Megalodesulfovibrio gigas
the native enzyme contains 0.03 mol zinc per mole of protein
Zn2+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Zn2+
Zn2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Zn2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Zn2+
-
residual activity even in the presence of EDTA
Zn2+
1 mol/mol recombinant enzyme
Zn2+
contains one Zn2+ per enzyme molecule. EDTA treatments of 1 h at 75°C or 80°C is necessary to deplete the enzyme from its Zn2+. Presence of four Zn2+ liganding cysteines. Zn2+ is not necessary for enzyme activity
additional information
the enzyme is not activated by Mn2+
additional information
-
the enzyme is not activated by Mn2+
additional information
-
no activation by Sr2+