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Information on EC 2.7.6.4 - nucleotide diphosphokinase
for references in articles please use BRENDA:EC2.7.6.4
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.6 Diphosphotransferases
2.7.6.4 nucleotide diphosphokinase
IUBMB Comments
The enzyme acts on the 5′-mono-, di- and triphosphate derivatives of purine nucleosides.
The expected taxonomic range for this enzyme is: Streptomyces
showSynonyms
nucleotide pyrophosphotransferase, nucleotide diphosphokinase, nucleotide 3'-pyrophosphokinase, atp nucleotide 3'-pyrophosphokinase, nucleotide pyrophosphokinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP nucleotide 3'-pyrophosphokinase
-
-
-
-
ATP:nucleotide pyrophosphotransferase
-
-
-
-
nucleotide 3'-pyrophosphokinase
-
-
-
-
nucleotide pyrophosphokinase
-
-
-
-
nucleotide pyrophosphotransferase
-
-
-
-
pyrophosphokinase, nucleotide
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside 3'-diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diphosphate transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:nucleoside-5'-phosphate diphosphotransferase
The enzyme acts on the 5'-mono-, di- and triphosphate derivatives of purine nucleosides.
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CAS REGISTRY NUMBER
COMMENTARY
53167-92-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + IDP
AMP + inosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + IMP
AMP + inosine 3'-diphosphate 5'-phosphate
-
Substrates: -
Products: -
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?
ATP + ITP
AMP + inosine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
Products: -
?
dATP + AMP
dAMP + adenosine 3'-diphosphate 5'-phosphate
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Substrates: -
Products: -
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?
dATP + ATP
dAMP + adenosine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
Products: -
?
dATP + CTP
dAMP + cytidine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
Products: -
?
dATP + GMP
dAMP + guanosine 3'-diphosphate 5'-phosphate
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Substrates: -
Products: -
Products: -
?
dATP + IDP
dAMP + inosine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
Products: -
?
dATP + IMP
dAMP + inosine 3'-diphosphate 5'-phosphate
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Substrates: -
Products: -
Products: -
?
dATP + ITP
dAMP + inosine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
Products: -
?
dATP + UTP
dAMP + uridine 3'-diphosphate 5'-triphosphate
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Substrates: -
Products: -
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?
pppApp + GTP
pppGpp + ATP
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Substrates: 32.2% of the activity with GTP as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: dinucleotide 3',5'-diphosphodiester linkages, namely pAppA, ppAppA, and pppAppA are formed as transient intermediate during the diphosphokinase-catalyzed reaction of ApppA, AppppA, and ApppppA leading to the synthesis of pAp, ppAp and pppAp, which in turn is further converted to pAp, respectively
Products: -
Products: -
?
ATP
AMP + adenosine-3'-diphosphate-5'-triphosphate
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Substrates: -
Products: -
Products: -
?
ATP
AMP + adenosine-3'-diphosphate-5'-triphosphate
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Substrates: -
Products: -
Products: -
?
ATP
AMP + adenosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP
AMP + adenosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + ADP
AMP + adenosine 3'-diphosphate 5'-diphosphate
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Substrates: -
Products: -
Products: -
?
ATP + ADP
AMP + adenosine 3'-diphosphate 5'-diphosphate
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Substrates: -
Products: -
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?
ATP + ADP
AMP + adenosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + ADP
AMP + adenosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + AMP
AMP + adenosine 3'-phosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + AMP
AMP + adenosine 3'-phosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GMP
AMP + guanosine 3'-phosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GMP
AMP + guanosine 3'-phosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine-3'-diphosphate-5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + ADP
dAMP + adenosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + ADP
dAMP + adenosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GDP
dAMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GDP
dAMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GTP
dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GTP
dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GTP
dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: 40.2% of the activity with GTP as substrate
Products: -
Products: -
?
dATP + GTP
dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: 40.2% of the activity with GTP as substrate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
-
absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity
Zn2+
Co2+
-
absolute requirement for a divalent metal ion, at pH 10.0 Mg2+ and Mn2+ are most effective, at pH 7.0 Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
Co2+
-
absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity. Optimal concentration is 2.5 mM Co2+
Fe2+
-
absolute requirement for a divalent metal ion, at pH 10.0 Mg2+ and Mn2+ are most effective, at pH 7.0 Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
Fe2+
-
absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity
Mg2+
-
absolute requirement for a divalent metal ion, at pH 10.0, Mg2+ and Mn2+ are most effective. At pH 7.0, Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
Mg2+
-
absolute requirement for bivalent cations, at pH 10.0, Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity. Optimal concentration is 5 mM Mg2+
Mg2+
-
most actively stimulates at 30-100 mM, half-maximal activation from 10 to 100 mM
Mn2+
-
absolute requirement for a divalent metal ion, at pH 10.0 Mg2+ and Mn2+ are most effective, at pH 7.0 Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
Mn2+
-
absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity
Zn2+
-
absolute requirement for a divalent metal ion, at pH 10.0 Mg2+ and Mn2+ are most effective, at pH 7.0 Mg2+, Co2+, Mn2+, Fe2+ and Zn2+ are effective
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Leukemia, Myeloid, Acute
The prognostic value of cN-II and cN-III enzymes in adult acute myeloid leukemia.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 10.5
-
optimal pH with Mg2+ or Mn2+ as stimulating cation
7.5 - 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 55
-
40°C: 70% of maximal activity, 55°C: about 85% of maximal activity, pH 10.0
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the highest activity is obtained after 30-40 h cultivation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
24000
28000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
pH 9-11, in 0.05 M glycine/NaOH buffer containing 0.01 M MgCl2, no significant loss of activity after 15 min
37
-
pH 7-11, 37°C, over 90% of the original activity is retained after 2 h
40
-
10 min, 50% loss of original activity, inactivation is prevented by addition of substrate, non-ionic surface active agents or protein
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at low protein concentration, below 0.01 mg/ml, considerable loss in activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.05 M glycine/NaOH buffer, pH 9.0, 0.01 M MgCl2, in 60% saturated ammonium sulfate, 1 mg protein per mol, stable for at least several months
-
no measurable loss of activity is detected after several months in a refrigerator
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishino, T.; Murao, S.
Purification and some properties of ATP:nucleotide pyrophosphotransferase of Streptomyces adephospholyticus
Agric. Biol. Chem.
38
2491-2496
1974
Streptomyces adephospholyticus, Streptomyces adephospholyticus A-4668
-
brenda
Murao, S.; Nishino, T.
Isolation and identification of ATP:nucleotide pyrophosphotransferase-producing microorganism
Agric. Biol. Chem.
38
2483-2489
1974
Streptomyces adephospholyticus
-
brenda
Nishino, T.; Murao, S.
Physicochemical and enzymatic properties of ATP:nucleotide pyrophosphotransferase
Agric. Biol. Chem.
39
1827-1833
1975
Streptomyces adephospholyticus
-
brenda
Mukai, J.I.; Hirashima, A.; Mikuniya, T.
Nucleotide 2',3'-cyclic monophosphokinase action of Streptomyces nucleotide 3'-pyrophosphokinase
Agric. Biol. Chem.
55
117-122
1991
Streptomyces morookaense
-
brenda
Murao, S.; Nishino, T.; Hamagishi, Y.
Synthesis of guanosine-3'-diphosphate-5'-diphosphate by nucleotide pyrophosphotransferase
Agric. Biol. Chem.
38
887-889
1974
Streptomyces adephospholyticus
-
brenda
Oki, T.; Yoshimoto, A.; Sato, S.; Takamatsu, A.
Purine nucleotide pyrophosphotransferase from Streptomyces morookaensis, capable of synthesizing pppApp and pppGpp
Biochim. Biophys. Acta
410
262-272
1975
Streptomyces morookaense, Streptomyces morookaense ATCC 19166
brenda
Mukai, J.I.; Kukita, T.; Murao, S.; Nishino, T.
Acceptor specificity of ATP:nucleoside-5-phosphate pyrophosphotransferase from Streptomyces adephospholyticus. Synthesis of the 3-pyrophosphates of pyrimidine nucleotides, some oligoribonucleotides, 5-diphosphonucleosidic coenzymes and mG-5-ppp-5-Am
J. Biochem.
83
1209-1212
1978
Streptomyces adephospholyticus, Streptomyces morookaense
brenda
Oki, T.; Yoshimoto, A.; Ogasawara, T.; Sato, S.; Takamatsu, A.
Occurrence of pppApp-synthesizing activity in actinomycetes and isolation of purine nucleotide pyrophosphotransferase
Arch. Microbiol.
107
183-187
1976
Streptomyces aspergilloides, Streptomyces hachijoensis, Streptomyces morookaense, Streptomyces septatus, Streptomyces violascens
brenda
Nishino, T.; Murao, S.
Characterization of pyrophosphoryl transfer reaction of ATP:nucleotide pyrophosphotransferase
Agric. Biol. Chem.
39
1007-1014
1975
Streptomyces adephospholyticus
-
brenda
Higuchi, T.; Mikuniya, T.; Osoegawa, K.; Ezaki, S.; Sumichika, H.; Mizui, Y.; Shoji, T.; Kishihara, K.; Muta, S.; Kuhara, S.; Mukai, J.I.
Streptomyces ATP nucleotide 3'-pyrophosphokinase-gene cloning and sequence analysis
Biosci. Biotechnol. Biochem.
58
2182-2187
1994
Streptomyces morookaense
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.6.4)
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