Information on EC 2.7.4.B2 - polyphosphate-AMP phosphotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.4.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
polyphosphate-AMP phosphotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
AMP + (phosphate)n = ADP + (phosphate)n-1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate:AMP phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
110639-29-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
like, one isolate obtained from a laboratory sewage treatment plant, another isolate does not show PPT activity
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Manually annotated by BRENDA team
no activity in Aureobacterium saperdae
two isolates obtained from a laboratory sewage treatment plant
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-
Manually annotated by BRENDA team
no activity in Curtobacterium sp.
four isolates obtained from a laboratory sewage treatment plant
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-
Manually annotated by BRENDA team
no activity in Shewanella putrefaciens
like, one isolate obtained from a laboratory sewage treatment plant
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dAMP + (phosphate)n
2'-dADP + (phosphate)n-1
show the reaction diagram
2'-deoxy-AMP + [phosphate]n
2'-deoxy-ADP + [phosphate]n-1
show the reaction diagram
-
-
-
-
?
ADP + [phosphate]n
AMP + [phosphate]n+1
show the reaction diagram
AMP + (phosphate)n
ADP + (phosphate)n-1
show the reaction diagram
AMP + [phosphate]n
ADP + [phosphate]n-1
show the reaction diagram
CMP + [phosphate]n
CDP + [phosphate]n-1
show the reaction diagram
dAMP + [phosphate]n
dADP + [phosphate]n-1
show the reaction diagram
18% of the activity with AMP
-
-
?
dCMP + [phosphate]n
dCDP + [phosphate]n-1
show the reaction diagram
0.008% of the activity with AMP
-
-
?
dGMP + [phosphate]n
dGDP + [phosphate]n-1
show the reaction diagram
2.6% of the activity with AMP
-
-
?
GDP + [phosphate]n
GMP + [phosphate]n+1
show the reaction diagram
GMP + [phosphate]n
GDP + [phosphate]n-1
show the reaction diagram
IMP + [phosphate]n
IDP + [phosphate]n-1
show the reaction diagram
2.2% of the activity with AMP
-
-
?
TMP + [phosphate]n
TDP + [phosphate]n-1
show the reaction diagram
0.012% of the activity with AMP
-
-
?
UMP + [phosphate]n
UDP + [phosphate]n-1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + [phosphate]n
AMP + [phosphate]n+1
show the reaction diagram
AMP + (phosphate)n
ADP + (phosphate)n-1
show the reaction diagram
AMP + [phosphate]n
ADP + [phosphate]n-1
show the reaction diagram
GDP + [phosphate]n
GMP + [phosphate]n+1
show the reaction diagram
GMP + [phosphate]n
GDP + [phosphate]n-1
show the reaction diagram
Q83XD3
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-
-
r
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
other metal ions such as Mn2+, Fe2+, Ca2+, Cu2+, Zn2+, and Co2+ cannot enhance the activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
slightly inhibitory at 50 mM
ATP
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6 mM, 30% inhibition
diphosphate
Tetraphosphate
Triphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
(Phosphate)n
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pH and temperature not specified in the publication, polyphosphate with an average chain length of 35 phosphate groups
8.3
ADP
reverse reaction of polyphosphate synthesis, pH 8.0, 37C
0.26 - 0.58
AMP
4.4
GMP
recombinant PAP, pH 8.0, 37C
0.0008
[phosphate]n
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polyphosphate with an average chain length of 35 phosphate groups, pH 8.5, 30C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
151.7 - 166.7
AMP
35
GMP
Acinetobacter johnsonii
Q83XD3
recombinant PAP, pH 8.0, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
333.3 - 616.7
AMP
30
7.83
GMP
Acinetobacter johnsonii
Q83XD3
recombinant PAP, pH 8.0, 37C
162
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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inhibition kinetics, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00957
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pH and temperature not specified in the publication
0.01
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cell-free isolate, pH and temperature not specified in the publication
2.48
crude extract of recombinant Escherichia coli strain JM109, pH 8.0, 37C
12
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partially purified native enzyme, pH 8.0, 37C, ADP synthesis
24.9
purified recombinant PAP tetramer, pH 8.0, 37C
54.9
purified recombinant PAP dimer, pH 8.0, 37C
101.2
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purified native enzyme, pH 8.5, 30C
9570
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purified native enzyme, pH 7.4, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
8 - 9
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
6.5 - 9.5
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pH 6.5: about 40% of maximal activity, pH 9.5: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18 - 40
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18C: about 40% of maximal activity, 40C: optimum, 45C: no activity
30 - 50
the level of activity at 50C is 3.2fold and 1.8fold higher than that at 30C and 37C, respectively
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
purified recombinant enzyme, stable at
722513
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, about 50% loss of activity which is not due to freezing and thawing
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-20C, purified enzyme, 1 month, 50% activity remaining, activity loss is not due to freezing and thawing
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4C, membrane fraction, over 2 months, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; native enzyme 20.1fold by anion exchange, hydrophobic interaction, and affinity chromatography
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by gel filtration, separation from polyphosphate kinase activity
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native enzyme 1511fold from strain 210A by streptomycin sulfate precipitation, two steps of anion exchange chromatography, hydrophobic interaction chromatography, and gel filtration
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native enzyme 200fold by membrane fraction preparation and washing with detergent Triton X-100 and SB-12; partial
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recombinant pPAP2 dimer 22.1fold from Escherichia coli strain JM109 by ammonium sulfate fractionation, anion exchange and hydroxyapatite chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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sensitive method for detecting AMP by using polyphosphate(polyP)-AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii in conjugation with firefly luciferase. The method allows detection of AMP over the concentration range of 0.3-100 pmol per assay
diagnostics
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity
food industry
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity
synthesis
additional information
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity