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
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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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General Information
General Information on EC 2.7.2.1 - acetate kinase
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evolution
malfunction
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ackA mutants are unstable and rapidly accumulate suppressor mutations that inactivate suppressors SpxB or SpxR
metabolism
physiological function
additional information
residue Asn337 of ATP-ecoAK is particularly significant for the specificity to ATP. The 5 residues are highly conserved in 2625 PPi-ehiAK homologsue implying that almost all organisms have ATP-dependent acetate kinase, EC 2.7.2.1, rather than diphosphate-dependent acetate kinase, EC 2.7.2.12
evolution
the enzyme is found in anaerobic as well as aerobic bacteria and Archaea. The enzyme belongs to the ASKHA phosphotransferase family (acetate and sugar kinases/Hsc70/actin) and is the best candidate for the common ancestor of this family
evolution
the enzyme is found in anaerobic as well as aerobic bacteria and domain of Archaea, and play a central role in major link in the carbon cycle. The enzyme is also participated in the production of major amount o ATP in most of the fermentative anaerobes. The enzyme belongs to the phosphotransferases of the ASKHA (acetate and sugar kinases/Hsc70/actin) and the best candidate for the common ancestor of this family
evolution
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the enzyme is found in anaerobic as well as aerobic bacteria and Archaea. The enzyme belongs to the ASKHA phosphotransferase family (acetate and sugar kinases/Hsc70/actin) and is the best candidate for the common ancestor of this family
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the enzyme is involved in the postulated phosphoketolase pathway
metabolism
the enzyme plays a central role in major link in the carbon cycle. The enzyme also participates in the production of major amount of ATP in most of the fermentative anaerobes
metabolism
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the enzyme acts negatively upon acetyl phosphate-dependent phosphorylation of the response regulator CiaR
metabolism
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the enzyme plays a central role in major link in the carbon cycle. The enzyme also participates in the production of major amount of ATP in most of the fermentative anaerobes
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metabolism
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the enzyme is involved in the postulated phosphoketolase pathway
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acetate kinase is a key enzyme of acetate metabolism of anaerobes
physiological function
at a concentration of 2 mM acetate, the acetate kinase activity in cell extract of Methanosarcina mazei is not limiting the methane formation rate
physiological function
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
physiological function
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
physiological function
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Isozyme AckA2 has an important role under acetate-limiting conditions despite the lower activity. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
physiological function
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acetate kinase plays a significant role in energy production and catalyzes the formation of acetate from acetyl phosphate. The enzyme is involved in the synthesis of most of the ATP formed catabolically
physiological function
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acetate kinase plays a significant role in energy production and catalyzes the formation of acetate from acetyl phosphate. The enzyme is involved in the synthesis of most of the ATP formed catabolically
physiological function
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acetate kinase EutQ is required during anoxic growth of Salmonella enterica on ethanolamine and tetrathionate
physiological function
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acetate kinase plays a significant role in energy production and catalyzes the formation of acetate from acetyl phosphate. The enzyme is involved in the synthesis of most of the ATP formed catabolically
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physiological function
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acetate kinase plays a significant role in energy production and catalyzes the formation of acetate from acetyl phosphate. The enzyme is involved in the synthesis of most of the ATP formed catabolically
-
physiological function
-
at a concentration of 2 mM acetate, the acetate kinase activity in cell extract of Methanosarcina mazei is not limiting the methane formation rate
-
physiological function
-
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
physiological function
-
acetate kinase is a key enzyme of acetate metabolism of anaerobes
-
physiological function
-
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Isozyme AckA2 has an important role under acetate-limiting conditions despite the lower activity. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
-
physiological function
-
acetate kinase converts acetyl phosphate to acetate along with the generation of ATP in the pathway for mixed-acid fermentation in Lactococcus lactis. The reverse reaction yields acetyl phosphate for assimilation purposes. AckA1 is an order of magnitude more active than AckA2 in both reaction directions, but AckA2 has the highest affinity for acetate. Allosteric regulation of isozymes AckA1 and AckA2 and the pool sizes of the glycolytic intermediates are consistent with a switch from homolactic to mixed-acid fermentation upon slowing of the growth rate
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construction of the three-dimensional structure of the Escherichia coli acetate kinase by use of molecular homology modeling using the structure of the enzyme from Thermotoga maritima, overview
additional information
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construction of the three-dimensional structure of the Escherichia coli acetate kinase by use of molecular homology modeling using the structure of the enzyme from Thermotoga maritima, overview
additional information
salts bridges and cation-pi interactions in the enzyme, overview
additional information
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salts bridges and cation-pi interactions in the enzyme, overview
additional information
salts bridges and cation-pi interactions in the enzyme, overview
additional information
substrate-binding site structure and comparison with diphosphate-dependent acetate kinase, EC 2.7.2.12, overview
additional information
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substrate-binding site structure and comparison with diphosphate-dependent acetate kinase, EC 2.7.2.12, overview
additional information
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salts bridges and cation-pi interactions in the enzyme, overview
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