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 (Engineering
Engineering on EC 2.7.2.1 - acetate kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G332D
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
G333Q
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
I334M
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N213T
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N213T/G332D/E336L/T385N
site-directed mutagenesis, the mutant shows unaltered Km for ATP and highly reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
N337E
site-directed mutagenesis, the mutant shows increased Km for ATP and reduced ATP-dependent acetate kinase activity compared to the wild-type enzyme
G239A
14.5fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G239S
192fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G331A
15.2fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q
118fold reduced specific activity. The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q/I332M
the mutations result in substantial reductions in kcat compared to the wild type enzyme. In the acetate-forming direction, catalysis is reduced over 100fold, and in the acetyl phosphate-forming direction, kcat is reduced about 50fold. This alteration results in about 5fold increase in Km for ADP and ATP, and a 15fold increase in Km for acetate but no substantial change in the Km for acetyl phosphate
N211A
N211S
200fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
N211T
44fold reduced specific activity (with ATP as substrate). Mutant enzyme shows little change in percentage activity observed with CTP and ITP. Activity with TTP is greatly enhanced and nearly equal to that observed with ATP, whereas the reduction in activity with UTP is stronger than that observed with the N211A
R91K
additional information
N211A
6fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
additional information
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mutant with no enzymic activity, fails to grow in xylose minimal medium under anaerobic conditions but grows anaerobically with arabinose
additional information
development of a one-pot process of enzymatic synthesis of deoxythymidine-5'-triphosphate (5'-dTTP) employing whole cells of recombinant Escherichia coli coexpressing thymidylate kinase (TMKase, EC 2.7.4.9) and acetate kinase (ACKase). The relative residual specific activities of TMKase and ACKase, pretreated with 20 mM EDTA, are 94% and 96%, respectively. The yield of 5'-dTTP reaches above 94% from 5 mM 5'-dTMP and 15 mM acetyl phosphate catalyzed with intact cells of the recombinant strain pretreated with EDTA. The process is so effective that only 0.125 mM ATP is sufficient to deliver the phosphate group from acetyl phosphate to dTMP and dTDP
additional information
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development of a one-pot process of enzymatic synthesis of deoxythymidine-5'-triphosphate (5'-dTTP) employing whole cells of recombinant Escherichia coli coexpressing thymidylate kinase (TMKase, EC 2.7.4.9) and acetate kinase (ACKase). The relative residual specific activities of TMKase and ACKase, pretreated with 20 mM EDTA, are 94% and 96%, respectively. The yield of 5'-dTTP reaches above 94% from 5 mM 5'-dTMP and 15 mM acetyl phosphate catalyzed with intact cells of the recombinant strain pretreated with EDTA. The process is so effective that only 0.125 mM ATP is sufficient to deliver the phosphate group from acetyl phosphate to dTMP and dTDP
additional information
each of five candidate residue in Escherichia coli ATP-specific AK (ATP-ecoAK), which is unable to use diphosphate, is substituted with the respective diphosphate-ehiAK amino acid residue. Each variant ATP-ecoAK has an increased Km for ATP, indicating that the five residues are the determinants for the specificity to ATP in ATP-ecoAK
additional information
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each of five candidate residue in Escherichia coli ATP-specific AK (ATP-ecoAK), which is unable to use diphosphate, is substituted with the respective diphosphate-ehiAK amino acid residue. Each variant ATP-ecoAK has an increased Km for ATP, indicating that the five residues are the determinants for the specificity to ATP in ATP-ecoAK
