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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Bos taurus
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2.7.4.3 adenylate kinaseIUBMB Comments
Inorganic triphosphate can also act as donor.
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Word Map
- 2.7.4.3
- phosphoenolpyruvate
- adp
- creatine
- hpr
- fructose
- nucleoside
-
permease
- streptococcus
-
phosphoenolpyruvate-dependent
- mannose
- 6-phosphate
-
catabolite
- deaminase
- lactose
- mannitol
- hexokinase
- mutans
- glucose-6-phosphate
-
camp-dependent
- aminoglycoside
- autophosphorylation
- phosphoglucomutase
-
phosphofructokinase
- kanamycin
- neomycin
- 6-phosphogluconate
-
phosphorelay
- 5'-nucleotidase
-
antiterminator
- mgatp
- 2-deoxyglucose
-
intermembrane
-
transphosphorylation
-
gamma-phosphate
- melibiose
- salivarius
- ganciclovir
- phosphocreatine
- nptii
-
diadenosine
-
diphosphohydrolase
-
gamma-32patp
-
p-loop
-
2.7.3.2
- dikinase
-
coarse-grained
- analysis
- phosvitin
- medicine
-
2,6-bisphosphate
- mucolipidosis
- phosphoenzyme
- diagnostics
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphotransferase, adenylate kinase, myokinase, adenylate kinase 1, adenylate kinase 2, nonstructural protein 4b, cinap, adenylokinase, spadk, adenylate kinase isoenzyme 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-AMP-kinase
-
-
-
-
adenylic kinase
-
-
-
-
adenylokinase
-
-
-
-
kinase, adenylate (phosphorylating)
-
-
-
-
kinase, myo- (phosphorylating)
-
-
-
-
myokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9013-02-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
Ca2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mn2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.1
8.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KAD5_BOVIN
562
0
63273
Swiss-Prot
other Location (Reliability: 2)
KAD6_BOVIN
172
0
19927
Swiss-Prot
other Location (Reliability: 3)
KAD2_BOVIN
241
0
26497
Swiss-Prot
other Location (Reliability: 2)
KAD1_BOVIN
194
0
21664
Swiss-Prot
other Location (Reliability: 1)
A0A3Q1N2Q9_BOVIN
230
0
25195
TrEMBL
Mitochondrion (Reliability: 4)
A0A3Q1MMK0_BOVIN
270
0
30461
TrEMBL
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison of amino acid composition of different sources
additional information
-
comparison of amino acid composition of different sources
additional information
-
a great deal of homology and some distinct differences between liver and muscle type enzymes of different organisms
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
method for simultaneous detection of adenylate kinase isoforms directly on gel or nitrocellulose after separation by denaturing electrophoresis and electroblotting. Method allows for quantitative dection of enzyme activity from amny sources in both its reaction courses
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
70% loss of activity at pH 5 in 50 mM acetate buffer and 30% loss of activity at pH 6 in phosphate buffer, at 4°C overnight
642589
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PMSF and 5'-AMP stabilize the bovine liver enzyme, 5'-AMP stabilizes the rabbit muscle enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
method for simultaneous detection of adenylate kinase isoforms directly on gel or nitrocellulose after separation by denaturing electrophoresis and electroblotting. Method allows for quantitative dection of enzyme activity from amny sources in both its reaction courses
analysis
detection of adenylate kinase isoforms directly on gel or nitrocellulose after separation by denaturing electrophoresis and electroblotting. Method allows to clarify the apparent molecular weights of most of those enzymes that follow the reaction of AMP plus MgATP and is alos quantitative. GTP:AMP phosphotransferase are not detectable
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noda, L.
Adenylate kinase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
8
279-305
1973
Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Citrus limon, Blattidae, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus, Physarum polycephalum, Rattus norvegicus, Sus scrofa, Thiobacillus denitrificans, Triticum aestivum
-
Kuby, S.A.; Fleming, G.; Frischat, A.; Cress, M.C.; Hamada, M.
Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP-AMP transphosphorylases from muscle and liver
J. Biol. Chem.
258
1901-1907
1983
Bos taurus, Oryctolagus cuniculus, Homo sapiens
Hall, S.W.; Khn, H.
Purification and properties of guanylate kinase from bovine retinas and rod outer segments
Eur. J. Biochem.
161
551-556
1986
Bos taurus
Tomasselli, A.G.; Noda, L.H.
Mitochondrial ATP:AMP phosphotransferase from beef heart: purification and properties
Eur. J. Biochem.
103
481-491
1980
Bos taurus
Kuby, S.A.; Hamada, M.; Gerber, D.; Tsai, W.C.; Jacobs, H.K.; Cress, M.C.; Chua, G.K.; Fleming, G.; Wu, L.H.; Fischer, A.H.; Frischat, A.; Maland, L.
Studies on adenosine triphosphate transphosphorylases. Isolation and several properties of the crystalline calf ATP-AMP transphosphorylases (adenylate kinases) from muscle and liver and some observations on the rabbit muscle adenylate kinase
Arch. Biochem. Biophys.
187
34-52
1978
Bos taurus, Oryctolagus cuniculus
Terai, H.
Adenylate kinase from Pseudomonas denitrificans. I. Purification and antiserum inhibition
J. Biochem.
75
1027-1036
1974
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Pseudomonas denitrificans (nom. rej.), Rattus norvegicus
Hamada, M.; Kuby, S.A.
Studies on adenosine triphosphate transphosphorylases. XIII. Kinetic properties of the crystalline rabbit muscle ATP-AMP transphorphorylase (adenylate kinase) and a comparison with the crystalline calf muscle and liver adenylate kinases
Arch. Biochem. Biophys.
190
772-792
1978
Bos taurus, Oryctolagus cuniculus
Schlauderer, G.J.; Schulz, G.E.
The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments
Protein Sci.
5
434-441
1996
Bos taurus
Yan, H.; Tsai, M.D.
Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity
Adv. Enzymol. Relat. Areas Mol. Biol.
73
103-134
1999
Bacillus subtilis, Bos taurus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens
Ravera, S.; Musante, L.; Calzia, D.; Panfoli, I.; Bruschi, M.; Candiano, G.; Pepe, I.M.; Morelli, A.
Expression of adenylate kinase 1 in bovine retinal cytosol
Curr. Eye Res.
32
249-257
2007
Bos taurus (P00570), Bos taurus
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