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
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acetyl-coa
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cdc42
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methanosarcina
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thermophila
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sludge
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acetogenic
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cdc42-associated
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acetylphosphate
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formate-lyase
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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
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butyryl-coa
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embden-meyerhof-parnas
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acetate-activating
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synthesis
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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
2.7.2.1 acetate kinaseAdvanced search results
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results (Specific Activity
Specific Activity on EC 2.7.2.1 - acetate kinase
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SPECIFIC ACTIVITY [µmol/min/mg] 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1750
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acetate kinase EutP, with GTP as cosubstrate, at 40°C, pH not specified in the publication
2400
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acetate kinase EutP, with ATP as cosubstrate, at 40°C, pH not specified in the publication
251
isolated enzyme, pH 7.0, temperature not specified in the publication
7
cell lysate, pH 7.0, temperature not specified in the publication
additional information
additional information
catalytic mechanism analyzed in wild-type and mutant variants, binding constants for the nucleotide substrates indicate that Arg241 is involved in transition state stabilization and not directly involved in nucleotide recognition or binding, or in the domain closure required for catalysis, binding constants of the nucleotide substrates for Arg91 suggest that this residue has a role in transition state stabilization, evidence for domain motion dependent upon nucleotide ligand binding presented, suggestion that Arg91 is important for closure of domain I onto domain II for catalysis
additional information
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catalytic mechanism analyzed in wild-type and mutant variants, binding constants for the nucleotide substrates indicate that Arg241 is involved in transition state stabilization and not directly involved in nucleotide recognition or binding, or in the domain closure required for catalysis, binding constants of the nucleotide substrates for Arg91 suggest that this residue has a role in transition state stabilization, evidence for domain motion dependent upon nucleotide ligand binding presented, suggestion that Arg91 is important for closure of domain I onto domain II for catalysis
additional information
transcription initiation and regulation controlled in a carbon source dependent manner, ackA gene encoding acetate kinase is strongly expressed in the presence of glucose, promoter mapping by primer extension, promoter recognition sites studied by promoter deletion analysis, -35 region seems to be of minor importance
additional information
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transcription initiation and regulation controlled in a carbon source dependent manner, ackA gene encoding acetate kinase is strongly expressed in the presence of glucose, promoter mapping by primer extension, promoter recognition sites studied by promoter deletion analysis, -35 region seems to be of minor importance
additional information
continuous assay, spectrophotometric quantification of phosphate achieved through measurement of the phosphorylysis of 2-amino-6-mercapto-7-methyl-purine riboside (MESG) to ribose-1-phosphate and 2-amino-6-mercapto-7-methyl-purine (MES) by purine nucleoside phosphorylase, sensitivity of the assay is in the range of 2-150 microM
additional information
-
continuous assay, spectrophotometric quantification of phosphate achieved through measurement of the phosphorylysis of 2-amino-6-mercapto-7-methyl-purine riboside (MESG) to ribose-1-phosphate and 2-amino-6-mercapto-7-methyl-purine (MES) by purine nucleoside phosphorylase, sensitivity of the assay is in the range of 2-150 microM
