EC Number   |
General Information |
Reference |
|---|
   2.7.4.33 | evolution |
polyphosphate kinases, responsible for the synthesis and utilization of polyphosphate, are divided into two families (PPK1 and PPK2) due to differences in amino acid sequence and kinetic properties. Phylogenetic analysis suggests that the PPK2 family is divided into three subfamilies (classes I, II, and III). Class I and II PPK2s catalyze nucleoside diphosphate and nucleoside monophosphate phosphorylation, respectively. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation synthesizing ATP from AMP. Class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. Class III PPK2 possesses both class I and II activities. The class III subfamily is closest to a PPK2 ancestor, overview |
-, 737499 |
| 2.7.4.33 | more |
ATP regeneration from AMP and polyphophate using PPT, firefly luciferase and hexokinase as model ATP-requiring enzymes, ADP can be converted to ATP by adenylate kinase, AdK. Establishment of a PPT/AdK system for ATP regeneration with coupled hexokinase, overview |
-, 718620 |
| 2.7.4.33 | more |
overexpression in strain PAO1 leads to a massive production of polyphosphate kinase, PPK, and a marked enhancement of polyphosphate-synthesizing activity, while the PAP activity is not affected by overproduction of PPK |
718728 |
| 2.7.4.33 | more |
PAP contains two putative phosphate-binding motifs, P-loops. The similarity between PAP and the PPK2 homologues indicates that there is a common mechanism by which these enzymes use poly(P) for phosphorylation of nucleosides. The C-terminal region of PAP, including one P-loop (amino acids 286 to 292), is thought to be essential for poly(P)-dependent nucleotide phosphorylation. An additional P-loop in the N-terminal region (amino acids 45 to 51) of PAP may play a crucial role in binding with nucleoside monophosphate |
-, 722513 |
| 2.7.4.33 | more |
polyphosphate kinase, PPK, responsible for the processive synthesis of inorganic polyphosphate from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyphosphate to ADP to yield ATP. When coexpressed with adenylate kinase, ADK, in Escherichia coli, PPK and ADK together highly enhance the PAP activity in Escherichia coli |
-, 720883 |
| 2.7.4.33 | more |
residue E126 is important for class III PPK2 activity. Structure homology modeling using the Arthrobacter aurescens PPK2 enzyme (PDB ID 3RHF) sequence as template |
-, 737499 |
| 2.7.4.33 | physiological function |
enzyme PPK2 catalyzes preferentially polyphosphate-driven nucleotide phosphorylation (utilization of polyphosphate), which is important for the survival of microbial cells under conditions of stress or pathogenesis. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation, synthesizing ATP from AMP by a single enzyme |
-, 737499 |
| 2.7.4.33 | physiological function |
PPT from Acinetobacter johnsonii is specific for AMP and 2'-dAMP |
-, 718620 |
| 2.7.4.33 | physiological function |
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani |
-, 738411 |
| 2.7.4.33 | physiological function |
the inhibition of polyphosphate:AMP phosphotransferase-mediated degradation by diphosphate and triphosphate is abolished by the inorganic diphosphatase, EC 3.6.1.1 |
-, 721769 |
