EC Number |
General Information |
Reference |
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2.7.2.1 | evolution |
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 |
738717 |
2.7.2.1 | 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 |
-, 739591 |
2.7.2.1 | 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 |
739591 |
2.7.2.1 | malfunction |
ackA mutants are unstable and rapidly accumulate suppressor mutations that inactivate suppressors SpxB or SpxR |
722528 |
2.7.2.1 | metabolism |
the enzyme acts negatively upon acetyl phosphate-dependent phosphorylation of the response regulator CiaR |
761854 |
2.7.2.1 | metabolism |
the enzyme is involved in the postulated phosphoketolase pathway |
-, 737465 |
2.7.2.1 | 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 |
-, 739591 |
2.7.2.1 | more |
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 |
738854 |
2.7.2.1 | more |
salts bridges and cation-pi interactions in the enzyme, overview |
-, 739591 |
2.7.2.1 | more |
substrate-binding site structure and comparison with diphosphate-dependent acetate kinase, EC 2.7.2.12, overview |
738717 |