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Enzyme Nomenclature
Information on EC 2.7.4.3 - adenylate kinase
for references in articles please use BRENDA:EC2.7.4.3
Word Map on EC 2.7.4.3
- 2.7.4.3
- pt
- phosphoenolpyruvate
- adp
- creatine
- fructose
-
permease
- nucleoside
- streptococcus
- subtilis
-
phosphoenolpyruvate-dependent
- mannose
-
catabolite
-
6-phosphate
- deaminase
- hexokinase
- lactose
- mannitol
- mutans
-
autophosphorylation
- glucose-6-phosphate
- phosphoglucomutase
-
camp-dependent
-
aminoglycoside
- 5'-nucleotidase
- 2-deoxyglucose
- kanamycin
-
phosphofructokinase
-
intermembrane
- 6-phosphogluconate
-
phosphorelay
-
diadenosine
-
antiterminator
- salivarius
- ganciclovir
-
transphosphorylation
- mgatp
-
p-loop
-
gamma-phosphate
- phosphocreatine
- adpase
-
phosvitin
-
2,6-bisphosphate
-
nptii
-
diphosphohydrolase
-
2.7.3.2
-
coarse-grained
-
dikinase
- mucolipidosis
- melibiose
- fructokinase
- analysis
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.4.3
-
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RECOMMENDED NAME
GeneOntology No.
adenylate kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
triphosphate can also act as donor
-
-
-
ATP + AMP = 2 ADP
mechanism
-
ATP + AMP = 2 ADP
binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites
-
ATP + AMP = 2 ADP
coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
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CAS REGISTRY NUMBER
COMMENTARY
9013-02-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DNA repair complex components Mre11 and Rad50 show adenylate kinase activity when in complex Mre11/Rad50
-
-
construction of chimera between the mesophilic Bacillus subtilis enzyme and the thermophilic Bacillus stearothermophilus enzyme
-
-
-
642558, 642583, 642586, 642616, 642617, 642623, 642625, 642626, 660819, 675337, 689928, 691500, 695156, 702283, 702705, 703676, 704583, 705166, 705341, 738750
-
-
-
UniProt
-
642558, 642563, 642564, 642565, 642566, 642567, 642589, 642603, 642623, 663243, 673004, 690717, 691336, 691397, 704723, 705850, 705851, 722394, 734231, 738750
-
-
adenylate kinase-deficient patients with chronic hemolytic anemia; isoform 1; patients deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia
SwissProt
DNA repair complex components Mre11 and Rad50 show adenylate kinase activity when in complex Mre11/Rad50; Mre11/Rad50 complex, part of a DNA repair complex
-
-
patients with limbic encephalitis refractory to corticosteroids, IVIg and plasma exchange
-
-
-
642556, 642558, 642560, 642566, 642573, 642589, 642596, 642597, 642598, 642599, 642605, 642610, 642611, 642613, 642618, 642622, 642623, 674609, 675108, 701686, 704850
-
-
DNA repair complex components Mre11 and Rad50 show adenylate kinase activity when in complex Mre11/Rad50; Mre11/Rad50 complex, part of a DNA repair complex
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
physiological function
additional information
malfunction
although homozygous adenylate kinsase 2 mutated embryos develop without any visible defects, their growth ceases and they die before reaching the third instar larval stage
malfunction
-
reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2
malfunction
-
adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness
malfunction
-
adenylate kinase 2 knockdown in larvae by RNA interference causes larval growth defects, including body weight decrease and development delay. Adenylate kinase 2 knockdown in larvae also decreases the number of circulating hemocytes
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
malfunction
-
the absence of denylate kinase 6 reduces stem elongation but does not delay development
malfunction
rrecombinant expression of wild-type adk gene in fucose-inducible strains rescues a growth defect, but expression of the Arg89 mutant does not. Lack of functional SpAdK causes a growth defect in vivo, SpAdK deficiency abolishes pneumococcal growth
physiological function
-
adenylate kinase 4 is a unique member of the adenylate kinases family which shows no enzymatic activity in vitro
physiological function
maternally provided adenylate kianse 2 is sufficient for embryonic development, adenylate kinase 2 plays a critical role in adenine nucleotide metabolism in the mitochondrial intermembrane space and is essential for growth in Drosophila melanogaster
physiological function
-
adenylate kinase 2 regulates cell growth, viability, and proliferation in insect growth and development
physiological function
-
adenylate kinase 6 is an essential stem growth factor in Arabidopsis
physiological function
-
nuclear adenylate kinase isoform is involved in ribosome biogenesis by performing ribosomal 18S RNA processing by direct interaction with ribosomal protein TcRps14
physiological function
adenylate kinases play a critical role in intercellular homeostasis by the interconversion of ATP and AMP to two ADP molecules
physiological function
SpAdK plays an essential role in pneumococcal growth and ATP synthesis, the enzyme is essential for growth through its catalytic activity, it controls cell growth via cellular energy homeostasis. SpAdK increases total cellular ATP levels regulated by fucose in the fucose-inducible strain
additional information
-
ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. The active center of an adenylate kinase comprises separate ATP- and AMP-binding sites, and comprises ATP-binding site 2. Construction of a three-dimensional model of the CFTR NBD1-NBD2 heterodimer, molecular modelling with bound ATP molecules, overview
additional information
the ligand-free enzyme structure reveals an open conformation
additional information
Arg89 is a key active site residue, enzyme structure comparisons
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ANK, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ZIN, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 2BBW, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1DVR, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
additional information
-
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
-
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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
1,N6-ethenoadenosine 5'-triphosphate + AMP
? + ADP
-
not ATP + 1,N6-ethenoadenosine 5'monophosphate
-
-
ir
2 ADP
ATP + AMP
pfSMCnbd possesses reverse adenylate kinase activity. In adenylate kinase reactions, ATP binds to its canonical binding site while AMP binds to the Q-loop glutamine and a hydration water of the Mg2+ ion. Furthermore, mutational analysis indicates that adenylate kinase reaction occurs in the engaged pfSMCnbd dimer and requires the Signature motif for phosphate transfer
-
-
?
adenosine 5'-(3-thio)triphosphate + AMP
adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
-
muscle: reaction at 97% the rate of ATP, liver mitochondria: reaction at 70% the rate of ATP
-
-
?
ADP + diphosphate
ATP + phosphate
-
at 0.1% the rate of the natural substrates
-
-
?
ATP + 7-deazaadenosine 5'-monophosphate
ADP + 7-deazaadenosine 5'-diphosphate
-
i.e. tubercidine monophosphate
-
-
?
ATP + adenine-9-beta-D-arabinofuranoside 5'-monophosphate
ADP + adenine-9-beta-D-arabinofuranoside 5'-diphosphate
-
-
-
-
?
ATP + adenosine 5'-thiophosphate
?
-
muscle: reaction at 56% the rate of AMP, liver mitochondria: reaction at 95% the rate of AMP
-
-
?
ATP + AMP-3'-diphosphate
?
-
muscle: reaction at 57% the rate of AMP, liver mitochondria: reaction at 86% the rate of AMP
-
-
?
ATP + CDP
ADP + CTP
-
-
nucleoside triphosphate synthesis by beta-phosphoryl transfer from ADP to any bound nucleoside diphosphate
-
r
ATP + shikimic acid
ADP + ?
shikimic acid is a good substrate
-
-
?
dATP + dAMP
dADP + dADP
AMP and dAMP are the preferred substrates
-
-
?
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
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
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
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
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
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
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
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
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
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
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
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
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
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
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
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
ADP + ADP
?
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
ADP + ADP
ATP + AMP
-
no substrates: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
-
-
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + TDP
AMP + TTP
-
Escherichia coli adenylate kinase is able to synthesize TTP, but the activity is too low to explain the high rate of TTP accumulation uring amino acid starvation of cells
-
-
?
ADP + TDP
AMP + TTP
-
rate of TTP synthesis is more than 1000000fold lower than ATP synthesis
-
-
?
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
ADP
AMP and dAMP are the preferred substrates, ATP is the best phosphate donor
-
-
?
ATP + AMP
ADP + ADP
-
ATP is the preferred phosphate donor and AMP is the best phosphate acceptor
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrates are O1-AMP, epsilon-AMP, 8-bromo-AMP, 2',3'-dialdehyde-AMP
-
r
ATP + AMP
ADP + ADP
-
in addition to the hydrolysis of NTP and NDP substrates, adenylate kinase activity is detected in purified preparations of nonstructural protein 4B with the reverse reaction ADP + ADP -> ATP + AMP, yielding a larger kcat compared to that of the forward reaction ATP + AMP -> ADP + ADP
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrates are adenosine triphosphate 3'-diphosphate, adenosine-5'-(3-thio)triphosphate/adenosine 5'-thiophosphate
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
r
ATP + AMP
ADP + ADP
-
adenylate kinase 4 shows slightly lower efficiency for the phosphorylation of AMP with ATP compared to the phosphorylation of AMP with GTP
-
-
?
ATP + AMP
ADP + ADP
adenylate kinase 5 domain AK5p1, at the assay conditions used, and at lower concentrations of substrate, AK5p1 shows generally a higher affinity for AMP compared to dAMP
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrate of the reverse reaction: UDP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: adenosine tetraphosphate
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
substrates in decreasing order of activity, in the presence of Mn2+: ATP, 2'-dATP, CTP, GTP, UTP, ITP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
the adenylate kinase-catalyzed reaction requires a nucleotide complexed with Mg2+ as one substrate and a free nucleotide as the second substrate
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
the substrate pair ATP/AMP results in maximal activity
-
-
?
ATP + AMP
ADP + ADP
-
no substrates are 3',5'-cAMP, dAMP, 2'-AMP, 3'-AMP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
substrates in decreasing order of activity, in the presence of Mg2+: ATP, dATP, GTP, ITP
-
r
ATP + AMP
ADP + ADP
-
no substrates are adenosine, 2',3'-AMP or 3',5'-AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
no substrates are GTP/GMP, TTP/TMP
-
r
ATP + AMP
ADP + ADP
other NMP substrates are very poor acceptors
-
-
?
ATP + AMP
ADP + ADP
other NMP substrates are very poor acceptors
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + CMP
ADP + CDP
adenylate kinase 5 domain AK5p1, the relative efficiency of CMP is about 15% compared to AMP
-
-
?
ATP + CMP
ADP + CDP
-
phosphorylation of CMP is also detected but to a lesser extend
-
-
?
ATP + dCMP
ADP + dCDP
dCMP is a poor substrate, but preferred over IMP, UMP
-
-
?
ATP + dCMP
ADP + dCDP
adenylate kinase 5 domain AK5p1, the relative efficiency of dCMP is about 15% compared to AMP
-
-
?
dATP + AMP
dADP + ADP
AMP and dAMP are the preferred substrates, dATP is a good phosphate donor
-
-
?
GTP + AMP
GDP + ADP
-
isozyme adenylate kinase 4 shows its highest efficiency when phosphorylating AMP with GTP, when GTP is used as phosphate donor only AMP is clearly phosphorylated and the phosphorylation efficiency for dAMP, CMP and dCMP is very low
-
-
?
additional information
?
-
interaction between mitochondrial adenylate kinase and nucleoside diphosphate kinase. Adenylate kinase stimulates nucleoside diphosphate kinase activity, whereas nucleoside diphosphate kinase inhibits adenylate kinase activity. the net effect may be unchanged ADP production albeit with different rates of substrate consumption
-
-
-
additional information
?
-
-
the enzyme has broader specificity for NMPs than mammalian enzymes
-
-
-
additional information
?
-
-
adenylate kinase participates in the regulation of ADP-dependent endocytosis of high-density lipoprotein by consuming the ADP generated by the ecto-F1-ATPase
-
-
-
additional information
?
-
-
adenylate kinase activity of the Mre11/Rad50 complex, which is part of a DNA repair complex, promotes DNA-DNA associations
-
-
-
additional information
?
-
-
adenylate kinase 4 catalyzes the phosphorylation of AMP, dAMP,CMPand dCMP with ATP or GTP as phosphate donors and also phosphorylates AMP with UTP as phosphate donor
-
-
-
additional information
?
-
AK5p1 phosphorylates AMP, CMP, dAMP and dCMP with ATP or GTP as phosphate donors, AK5p2 phosphorylates AMP, CMP and dAMP when ATP is used as phosphate donor and AMP, CMP and dCMP with GTP as phosphate donor, AK5p2 cannot phosphorylate dAMP in the presence of GTP
-
-
-
additional information
?
-
CINAP has previously been designated as an adenylate kinase AK6, but is very atypical as it exhibits unusually broad substrate specificity, structural features characteristic of ATPase/GTPase proteins (Walker motifs A and B) and also intrinsic ATPase activity
-
-
-
additional information
?
-
-
the enzyme catalyzes the phosphorylation of AMP (highest affinity), dAMP, CMP and dCMP with ATP as phosphate donor, while only AMP and CMP are phosphorylated when GTP is the phosphate donor. With ATP or GTP as phosphate donor it was possible to detect the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP as enzymatic products from the corresponding diphosphate substrates
-
-
-
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides
-
-
-
additional information
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
additional information
?
-
monophosphates: IMP, GMP, CMP, UMP: activity below 1%
-
-
-
additional information
?
-
-
when replacing AMP by GMP, UMP or IMP the measured activity is less than 1%
-
-
-
additional information
?
-
when replacing AMP by GMP, UMP or IMP the measured activity is less than 1%
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
at the measured in vivo concentrations of ADP of 0.114 mM, at pH 7.6, the axonemal adenylate kinase could contribute31%, and creatine kinase 69%, of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme. The three catalytic domains of adenylate kinase are considerably divergent from each other
-
-
-
additional information
?
-
-
at the measured in vivo concentrations of ADP of 0.114 mM, at pH 7.6, the axonemal adenylate kinase could contribute31%, and creatine kinase 69%, of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme. The three catalytic domains of adenylate kinase are considerably divergent from each other
-
-
-
additional information
?
-
-
ATP + IMP 0.1% activity, ATP + GMP 0.3% activity
-
-
-
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + TDP
AMP + TTP
-
Escherichia coli adenylate kinase is able to synthesize TTP, but the activity is too low to explain the high rate of TTP accumulation uring amino acid starvation of cells
-
-
?
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
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
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
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
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
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
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
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
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
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
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
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
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
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
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
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
ADP + ADP
?
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
additional information
?
-
O82514
interaction between mitochondrial adenylate kinase and nucleoside diphosphate kinase. Adenylate kinase stimulates nucleoside diphosphate kinase activity, whereas nucleoside diphosphate kinase inhibits adenylate kinase activity. the net effect may be unchanged ADP production albeit with different rates of substrate consumption
-
-
-
additional information
?
-
-
adenylate kinase participates in the regulation of ADP-dependent endocytosis of high-density lipoprotein by consuming the ADP generated by the ecto-F1-ATPase
-
-
-
additional information
?
-
-
adenylate kinase activity of the Mre11/Rad50 complex, which is part of a DNA repair complex, promotes DNA-DNA associations
-
-
-
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides
-
-
-
additional information
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
the adenylate kinase protein preparation contains non-covalently bound ADP
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cobalt
Fe2+
K+
Li+
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
Mg2+
Mn2+
Na+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like Na+
NH4+
Zinc
Zn2+
additional information
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
Rhodopseudomonas rubrum
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ca2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+; less effective than Mg2+; metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Ca2+
the enzyme is slightly activated by Ca2+ (85% relative activity at 5 mM)
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+; metal ion forms complex with di- or trinucleotide; requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+; less effective than Mg2+; metal ion forms complex with di- or trinucleotide; requirement, as good as Mg2+
Ca2+
-
binding of substrates also takes place in the absence of metal ions; in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+; requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
Co2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Cobalt
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Cobalt
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Fe2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
K+
the enzyme is highly activated by K+, the optimal concentration is 10 mM
K+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like K+
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
the enzyme activity is highly dependent on Mg2+, and the optimal concentration of Mg2+ is 2 mM
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
direct Mg2+ binding activates adenylate kinase from Escherichia coli in addition to ATP-complexed Mg2+, Mg2+ can bind to adenylate kinase directly prior to AMP binding
Mg2+
-
MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
the adenylate kinase-catalyzed reaction requires a nucleotide complexed with Mg2+ as one substrate and a free nucleotide as the second substrate, maximum enzyme activity when [Mg2+]/[ATP] equals 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
binding of substrates also takes place in the absence of metal ions; in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+; inhibits at high concentrations; requirement
Mg2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; requirement; residual activity even in the presence of EDTA
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mn2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
binding of substrates also takes place in the absence of metal ions; Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
NH4+
the enzyme is highly activated by NH4+ (93.6% relative activity at 5 mM)
NH4+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like NH4+
Zinc
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Zn2+
-
0.8-1 mol Zn2+ for wild-type and mutants H138N, D153C and D153T, 0.6 mol Zn2+ for mutant D153T, or 0.34 mol Zn2+ for mutant C130H per mol protein, atomic absorption spectrophotometry
Zn2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Zn2+
-
requirement, tightly bound, 0.8 mol Zn2+ per mol protein, atomic absorption spectrophotometry
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
Zn2+
-
contains one Zn2+ per enzyme molecule. EDTA treatments of 1 h at 75°C or 80°C is necessary to deplete the enzyme from its Zn2+. Presence of four Zn2+ liganding cysteines. Zn2+ is not necessary for enzyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-deazaadenosine 5'-monophosphate
-
i.e. tubercidine 5'-monophosphate
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
Ag+
-
Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
cystine
-
adenylate kinase activity is diminished in the brain cortex of rats loaded with cystine dimethylester (0.0016 mg/g body weight), co-administration with cysteamine (0.00046 mg/g body weight) prevents inhibition of adenylate kinase caused by cystine
D-glucose
-
elevated concentrations of glucose inhibit cytosolic isoform AK1 expression. Inhibition of adenylate kinase increases the ATP/ADP ratio in the microenvironment of the K/ATP channel promoting channel closure and insulin secretion
P1,P4-bis(adenosine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P4-di(uridine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P5-(bis adenosine)-5'-pentaphosphate
inhibited activity of the recombinant enzyme, also inhibited the growth of L. donovani promastigotes in vitro
-
P1,P5-(diadenosine-5')-pentaphosphate
adenylate kinase-specific inhibitor
sulfur
-
elemental sulfur, reversible by dithiothreitol, muscle, not liver isozyme
suramin
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
uridine adenosine tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: mitochondrial enzyme; only cytosolic
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses; strong for muscle enzyme, less effective with dystrophic muscle or liver enzymes
8-anilino-1-naphthalenesulfonic acid
-
i.e. ANS, isoform N1 binds rapidly, isoform N2 converts to N1 and binds thereafter
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
ascorbate
-
at enzyme concentration above 200 nM, no inhibition. At concentrations below 200 nM, adenylate kinase becomes increasingly sensitive to ascorbate inhibition which is accompanied by a deviation from linear relatioship between enzyme concentration and activity to a concave relationship. Aldolase reverse inhibition by ascorbate
F-
Rhodopseudomona