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Literature summary extracted from

  • Resnick, S.M.; Zehnder, A.J.B.
    In vitro ATP regeneration from polyphosphate and AMP by polyphosphate:AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii 210A (2000), Appl. Environ. Microbiol., 66, 2045-2051.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.4.33 synthesis PPT catalyzes a key reaction in the cell-free regeneration of ATP from AMP and polyphosphate. The PPT/AdK system provides an alternative to existing enzymatic ATP regeneration systems in which phosphoenolpyruvate and acetylphosphate serve as phosphoryl donors and has the advantage that AMP and polyP are stable, inexpensive substrates Acinetobacter johnsonii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.33 Mg2+ required Acinetobacter johnsonii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.33 AMP + [phosphate]n Acinetobacter johnsonii
-
 ADP + [phosphate]n-1
-
 ?
2.7.4.33 AMP + [phosphate]n Acinetobacter johnsonii 210A
-
 ADP + [phosphate]n-1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.33 Acinetobacter johnsonii
-
-
-
2.7.4.33 Acinetobacter johnsonii 210A
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.33 2'-dAMP + (phosphate)n
-
 Acinetobacter johnsonii 2'-dADP + (phosphate)n-1
-
 ?
2.7.4.33 2'-dAMP + (phosphate)n
-
 Acinetobacter johnsonii 210A 2'-dADP + (phosphate)n-1
-
 ?
2.7.4.33 2'-deoxy-AMP + [phosphate]n
-
 Acinetobacter johnsonii 2'-deoxy-ADP + [phosphate]n-1
-
 ?
2.7.4.33 AMP + (phosphate)n
-
 Acinetobacter johnsonii ADP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + (phosphate)n
-
 Acinetobacter johnsonii 210A ADP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + [phosphate]n
-
 Acinetobacter johnsonii ADP + [phosphate]n-1
-
 ?
2.7.4.33 AMP + [phosphate]n
-
 Acinetobacter johnsonii 210A ADP + [phosphate]n-1
-
 ?
2.7.4.33 additional information GMP, UMP, CMP and IMP are not converted to the corresponding diphosphates Acinetobacter johnsonii ?
-
 ?
2.7.4.33 additional information PPT substrate specificity, overview. GMP, UMP, CMP, and IMP are not converted to the corresponding diphosphates at significant rates Acinetobacter johnsonii ?
-
 ?
2.7.4.33 additional information GMP, UMP, CMP and IMP are not converted to the corresponding diphosphates Acinetobacter johnsonii 210A ?
-
 ?
2.7.4.33 additional information PPT substrate specificity, overview. GMP, UMP, CMP, and IMP are not converted to the corresponding diphosphates at significant rates Acinetobacter johnsonii 210A ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.33 polyphosphate:AMP phosphotransferase
-
 Acinetobacter johnsonii
2.7.4.33 PPT
-
 Acinetobacter johnsonii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.33 35
-
 assay at Acinetobacter johnsonii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.33 7.6
-
 assay at Acinetobacter johnsonii

General Information

EC Number General Information Comment Organism
2.7.4.33 additional information 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 Acinetobacter johnsonii
2.7.4.33 physiological function PPT from Acinetobacter johnsonii is specific for AMP and 2'-dAMP Acinetobacter johnsonii