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Literature summary for 2.7.4.33 extracted from

  • Shiba, T.; Itoh, H.; Kameda, A.; Kobayashi, K.; Kawazoe, Y.; Noguchi, T.
    Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A (2005), J. Bacteriol., 187, 1859-1865.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.4.33

Cloned(Commentary)

Cloned (Comment) Organism
gene pap, construction of a cDNA library expressed in Escherichia coli, DNA and amino acid sequence determination and analysis, overexpression of pPAP2 from plasmid in Escherichia coli strain JM109 Acinetobacter johnsonii

Inhibitors

Inhibitors Comment Organism Structure
ammonium sulfate slightly inhibitory at 50 mM Acinetobacter johnsonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.27
-
 AMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii
0.45
-
 AMP recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4 Acinetobacter johnsonii
4.4
-
 GMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ specifically required, lowers the Km for the nucleotide substrate Acinetobacter johnsonii
additional information other metal ions such as Mn2+, Fe2+, Ca2+, Cu2+, Zn2+, and Co2+ cannot enhance the activity Acinetobacter johnsonii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55800
-
 x * 55800, recombinant pPAP2, SDS-PAGE Acinetobacter johnsonii

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Acinetobacter johnsonii Q83XD3 gene pap, plasmid containing the pap gene, designated pPAP2
-
Acinetobacter johnsonii 210A Q83XD3 gene pap, plasmid containing the pap gene, designated pPAP2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant pPAP2 dimer 22.1fold from Escherichia coli strain JM109 by ammonium sulfate fractionation, anion exchange and hydroxyapatite chromatography, and gel filtration Acinetobacter johnsonii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.48
-
 crude extract of recombinant Escherichia coli strain JM109, pH 8.0, 37°C Acinetobacter johnsonii
24.9
-
 purified recombinant PAP tetramer, pH 8.0, 37°C Acinetobacter johnsonii
54.9
-
 purified recombinant PAP dimer, pH 8.0, 37°C Acinetobacter johnsonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + [phosphate]n
-
 Acinetobacter johnsonii ADP + [phosphate]n-1
-
 ?
AMP + [phosphate]n best substrate Acinetobacter johnsonii ADP + [phosphate]n-1
-
 ?
AMP + [phosphate]n
-
 Acinetobacter johnsonii 210A ADP + [phosphate]n-1
-
 ?
AMP + [phosphate]n best substrate Acinetobacter johnsonii 210A ADP + [phosphate]n-1
-
 ?
CMP + [phosphate]n 0.09% of the activity with AMP Acinetobacter johnsonii CDP + [phosphate]n-1
-
 ?
CMP + [phosphate]n 0.09% of the activity with AMP Acinetobacter johnsonii 210A CDP + [phosphate]n-1
-
 ?
dAMP + [phosphate]n 18% of the activity with AMP Acinetobacter johnsonii dADP + [phosphate]n-1
-
 ?
dCMP + [phosphate]n 0.008% of the activity with AMP Acinetobacter johnsonii dCDP + [phosphate]n-1
-
 ?
dGMP + [phosphate]n 2.6% of the activity with AMP Acinetobacter johnsonii dGDP + [phosphate]n-1
-
 ?
GMP + [phosphate]n 10% of the activity with AMP Acinetobacter johnsonii GDP + [phosphate]n-1
-
 ?
GMP + [phosphate]n 10% of the activity with AMP Acinetobacter johnsonii 210A GDP + [phosphate]n-1
-
 ?
IMP + [phosphate]n 2.2% of the activity with AMP Acinetobacter johnsonii IDP + [phosphate]n-1
-
 ?
additional information PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively Acinetobacter johnsonii ?
-
 ?
additional information PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively Acinetobacter johnsonii 210A ?
-
 ?
TMP + [phosphate]n 0.012% of the activity with AMP Acinetobacter johnsonii TDP + [phosphate]n-1
-
 ?
UMP + [phosphate]n 0.13% of the activity with AMP Acinetobacter johnsonii UDP + [phosphate]n-1
-
 ?

Subunits

Subunits Comment Organism
? x * 55800, recombinant pPAP2, SDS-PAGE Acinetobacter johnsonii

Synonyms

Synonyms Comment Organism
PAP
-
 Acinetobacter johnsonii
polyphosphate:AMP phosphotransferase
-
 Acinetobacter johnsonii
pPAP2
-
 Acinetobacter johnsonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 recombinant enzyme Acinetobacter johnsonii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50 the level of activity at 50°C is 3.2fold and 1.8fold higher than that at 30°C and 37°C, respectively Acinetobacter johnsonii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 purified recombinant PAP, 10 min, 40% activity remaining without polyphosphate, 85% activity remaining in presence of 10 mM polyphosphate Acinetobacter johnsonii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
35
-
 GMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii
151.7
-
 AMP recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4 Acinetobacter johnsonii
166.7
-
 AMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 recombinant enzyme Acinetobacter johnsonii

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 11 purified recombinant enzyme, stable at Acinetobacter johnsonii

General Information

General Information Comment Organism
additional information 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 Acinetobacter johnsonii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7.83
-
 GMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii
333.3
-
 AMP recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4 Acinetobacter johnsonii
616.7
-
 AMP recombinant PAP, pH 8.0, 37°C Acinetobacter johnsonii