2.7.2.1: acetate kinase
This is an abbreviated version!
For detailed information about acetate kinase, go to the full flat file.
Word Map on EC 2.7.2.1
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2.7.2.1
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phosphotransacetylase
-
acetyl-coa
-
cdc42
-
methanosarcina
-
thermophila
-
sludge
-
acetogenic
-
cdc42-associated
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acetylphosphate
-
formate-lyase
-
non-receptor
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acetobutylicum
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substrate-level
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acetoin
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tyrobutyricum
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adp-forming
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phosphoketolase
-
butyryl-coa
-
embden-meyerhof-parnas
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acetate-activating
-
synthesis
-
industry
- 2.7.2.1
- phosphotransacetylase
- acetyl-coa
- cdc42
- methanosarcina
- thermophila
- sludge
-
acetogenic
-
cdc42-associated
- acetylphosphate
- formate-lyase
-
non-receptor
- acetobutylicum
-
substrate-level
- acetoin
- tyrobutyricum
-
adp-forming
- phosphoketolase
- butyryl-coa
-
embden-meyerhof-parnas
-
acetate-activating
- synthesis
- industry
Reaction
Synonyms
acetate kinase (phosphorylating), acetic kinase, acetokinase, ACK, ackA, AckA1, AckA2, ACKase, AK, ATP-ecoAK, ATP-specific AK, EAK, EutP, EutQ, MM_0495, Sak, short chain fatty acid kinase, StAckA, urkinase
ECTree
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Metals Ions
Metals Ions on EC 2.7.2.1 - acetate kinase
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Ca2+
Co2+
K+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Co2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Co2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Co2+
Vmax: 15%, compared to Mg2+ or Mn2+
Mg2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mg2+
binding constants of enzyme variants with ADP measured
Mg2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Mg2+
dependence on Mg2+ or Mn2+ ions, Km values is 0.28 mM
Mg2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Mg2+
1.3 mM used in assay conditions. The activity of the enzyme in the presence of Mg2+ is about 80% of that in the presence of Mn2+
Mn2+
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10 mM used in assay conditions. The enzyme exhibits about 25% higher specific activity with manganese as a cofactor compared to magnesium
Mn2+
the enzyme requires monovalent K+ and divalent Mn2+or Mg2+ cations
Mn2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). The maximum rate is obtained with Mn2+
Mn2+
dependence on Mg2+ or Mn2+ ions, Km values is 0.47 mM
Mn2+
the activity is strongly dependent on Mg2+ (100%), Mn2+ (100%) or Co2+ (68 %) ions
Ni2+
Vmax: 5%, compared to Mg2+ or Mn2+
additional information
-
Co2+, Ca2+, Cd2+ and Zn2+ can replace Mg2+ or Mn2+ only partially
additional information
no activity with Ba2+, Ca2+, Zn2+, or Cu2+
additional information
-
no activity with Ba2+, Ca2+, Zn2+, or Cu2+
additional information
-
no activity with Cu2+, Ni2+, Hg2+, Ba2+ or Fe2+