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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Mus musculus and UniProt Accession Q9R0Y5

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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This record set is specific for:
Mus musculus
UNIPROT: Q9R0Y5
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-AMP-kinase
-
-
-
-
adenylate kinase 2
-
-
adenylic kinase
-
-
-
-
adenylokinase
-
-
-
-
cystic fibrosis transmembrane conductance regulator
-
kinase, adenylate (phosphorylating)
-
-
-
-
kinase, myo- (phosphorylating)
-
-
-
-
myokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-02-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
show the reaction diagram
-
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
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
-
r
AMP + H2O
ADP + phosphate
show the reaction diagram
GMP can not be substituted for the AMP substrate
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
show the reaction diagram
-
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Mn2+
-
forms complex with di- or trinucleotide
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-(beta,gamma-imido)triphosphate tetralithium
-
non-metabolizable ATP analogue, inhibition of adenylate kinase abolishes the stimulatory effect of AMP on K/ATP channels
diadenosine polyphosphate
inhibits adenylate kinase activity of the nucleotide-binding domain 1 of CFTR
-
P1,P5-di(adenosine-5')pentaphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 0.45
ADP
0.03 - 0.07
AMP
0.000063 - 0.08
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.9
wild type, with AMP
1
G551D mutant, with ADP
1.2
wild type, with ATP
1.4
wild type, with ADP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform AK1
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression is upregulated during late spermiogenesis when the flagellum is being assembled
Manually annotated by BRENDA team
-
expression level of adenylate kinase 1 and ATP synthase beta is strongly increased during myogenesis
Manually annotated by BRENDA team
mRNA is present at low but relatively equivalent levels in pachytene spermatocytes, round spermatids, and condensing spermatids
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoenzyme AK1b
-
Manually annotated by BRENDA team
-
cytoplasmic adenylate kinase 1 is secreted from myotubes but not from myoblasts
-
Manually annotated by BRENDA team
-
isoenzyme AK1b
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
depletion of adenylate kinase 2 (AK2) by RNAi impairs adiponectin secretion in 3T3-L1 adipocytes, immunoglobulin M secretion in BCL1 cells, and the induction of the unfolded protein response during differentiation of both cell types. Depletion of AK2 results in changes in adipocyte energy homeostasis, but these effects do not detectably impair key adipocyte properties such as mitochondrial biogenesis and triglyceride storage
metabolism
-
adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KAD1_MOUSE
194
0
21540
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
x * 22000, SDS-PAGE
22000
-
2 * 22000 isoenzyme AK1, SDS-PAGE
23000
-
2 * 23000 isoenzyme AK1b, SDS-PAGE
28000
x * 28000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 22000, SDS-PAGE
?
x * 28000, SDS-PAGE
dimer
homodimer
static light scattering
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G551D
mutation affects the ability of the nucleotide-binding domain 1 of CFTR to dimerize, has an exaggerated nonlinear phase compared with the wild type
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
stable for 2.5 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nucleotide-binding domain 1 of CFTR purified to homogeneity by nickel ion affinity chromatography, followed by Sepharose S200 gel filtration and a second nickel affinity step
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into vector pET28b and expressed in Escherichia coli BL21DE3pLys cells
expression in Cos-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adenylate kinase 2 is markedly induced during adipocyte and B cell differentiation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
medicine
-
knock out of the major isoform adenylate kinase 1 disrupts the synchrony between inorganic phosphate turnover at ATP-consuming sites and gamma-ATP exchange at ATP synthesis sites. This reduces energetic signal communication in the post-ischemic heart. Adenylate kinase 1 gene deletion blunts vascular adenylate kinase phosphotransfer, compromises the contractility-coronary flow relationship, and precipitates inadequate coronary reflow following ischemiareperfusion. Deficit in adenylate kinase activity abrogates AMP signal generation and reduces the vascular adenylate kinase/creatine kinase activity ratio essential for the response of metabolic sensors. The sarcolemma-associated splice variant adenylate kinase 1beta facilitates adenosine production. Adenosine treatment bypasseds adenylate kinase 1 deficiency and restores post-ischemic flow to wild-type levels
additional information
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
-
Manually annotated by BRENDA team
Janssen, E.; Kuiper, J.; Hodgson, D.; Zingman, L.V.; Alekseev, A.E.; Terzic, A.; Wieringa, B.
Two structurally distinct and spatially compartmentalized adenylate kinases are expressed from the AK1 gene in mouse brain
Mol. Cell. Biochem.
256/257
59-72
2004
Mus musculus
-
Manually annotated by BRENDA team
Cao, W.; Haig-Ladewig, L.; Gerton, G.L.; Moss, S.B.
Adenylate kinases 1 and 2 are part of the accessory structures in the mouse sperm flagellum
Biol. Reprod.
75
492-500
2006
Mus musculus (Q9R0Y5), Mus musculus (Q9WTP6), Mus musculus
Manually annotated by BRENDA team
Ravera, S.; Calzia, D.; Panfoli, I.; Pepe, I.M.; Morelli, A.
Simultaneous detection of molecular weight and activity of adenylate kinases after electrophoretic separation
Electrophoresis
28
291-300
2007
Mus musculus, Bos taurus (P00570)
Manually annotated by BRENDA team
Gross, C.H.; Abdul-Manan, N.; Fulghum, J.; Lippke, J.; Liu, X.; Prabhakar, P.; Brennan, D.; Willis, M.S.; Faerman, C.; Connelly, P.; Raybuck, S.; Moore, J.
Nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator, an ABC transporter, catalyze adenylate kinase activity but not ATP hydrolysis
J. Biol. Chem.
281
4058-4068
2006
Homo sapiens (P13569), Homo sapiens, Mus musculus (P26361), Mus musculus
Manually annotated by BRENDA team
Schulze, D.U.; Duefer, M.; Wieringa, B.; Krippeit-Drews, P.; Drews, G.
An adenylate kinase is involved in KATP channel regulation of mouse pancreatic beta cells
Diabetologia
50
2126-2134
2007
Mus musculus
Manually annotated by BRENDA team
Choo, H.J.; Kim, B.W.; Kwon, O.B.; Lee, C.S.; Choi, J.S.; Ko, Y.G.
Secretion of adenylate kinase 1 is required for extracellular ATP synthesis in C2C12 myotubes
Exp. Mol. Med.
40
220-228
2008
Mus musculus
Manually annotated by BRENDA team
Dzeja, P.P.; Bast, P.; Pucar, D.; Wieringa, B.; Terzic, A.
Defective metabolic signaling in adenylate kinase AK1 gene knock-out hearts compromises post-ischemic coronary reflow
J. Biol. Chem.
282
31366-31372
2007
Mus musculus
Manually annotated by BRENDA team
Burkart, A.; Shi, X.; Chouinard, M.; Corvera, S.
Adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
J. Biol. Chem.
286
4081-4089
2011
Mus musculus
Manually annotated by BRENDA team