Information on EC 2.7.4.3 - adenylate kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.4.3
-
RECOMMENDED NAME
GeneOntology No.
adenylate kinase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
show the reaction diagram
triphosphate can also act as donor
-
-
-
ATP + AMP = 2 ADP
show the reaction diagram
mechanism
-
ATP + AMP = 2 ADP
show the reaction diagram
mechanism
-
ATP + AMP = 2 ADP
show the reaction diagram
mechanism
-
ATP + AMP = 2 ADP
show the reaction diagram
thermodynamics and kinetics
-
ATP + AMP = 2 ADP
show the reaction diagram
iso-random bi-bi mechanism
-
ATP + AMP = 2 ADP
show the reaction diagram
mechanism
-
ATP + AMP = 2 ADP
show the reaction diagram
associative mechanism for phosphoryl transfer
-
ATP + AMP = 2 ADP
show the reaction diagram
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
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine ribonucleotides de novo biosynthesis
-
-
purine metabolism
-
-
Purine metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5'-AMP-kinase
-
-
-
-
AD-004 like protein
-
-
adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase
-
-
adenylate kinase 1
-
adenylate kinase 1
-
isoform
adenylate kinase 2
-
isoform
adenylate kinase 2
-
-
adenylate kinase 2
-
isoform
adenylate kinase 2
-
-
adenylate kinase 4
-
-
adenylate kinase 4
-
adenylate kinase 5
isozyme, human AK5 has two separate functional domains both having enzymatic activity
adenylate kinase 6
-
-
adenylate kinase 9
-
-
adenylate kinase isozyme 2
-
adenylate kinase-2
-
adenylate kinase-like protein 1
-
AKLP1
adenylic kinase
-
-
-
-
adenylokinase
-
-
-
-
ADK1
-
isoform
ADK2
-
isoform
AK1
-
isoform
AK2
-
isoform
AK2
-
isoform
AK4
isozyme
AK5
isozyme
AK5p1
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
AK5p2
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
ATP:AMP phosphotransferase
-
ATP:AMP phosphotransferase
-
ATP:AMP phosphotransferase
-
-
ATP:AMP phosphotransferase
-
-
coilin interacting nuclear ATPase protein
-
kinase, adenylate (phosphorylating)
-
-
-
-
kinase, myo- (phosphorylating)
-
-
-
-
myokinase
-
-
-
-
nonstructural protein 4B
-
possesses both adenylate kinase activity and nucleotide hydrolase activity
phosphotransferase
-
Saci_0573
locus name
Saci_0573
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9013-02-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform AK1
UniProt
Manually annotated by BRENDA team
isoform Amk2
UniProt
Manually annotated by BRENDA team
isoform Amk5
UniProt
Manually annotated by BRENDA team
construction of chimera between the mesophilic Bacillus subtilis enzyme and the thermophilic Bacillus stearothermophilus enzyme
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; soluble adenylate kinase isoform 1
SwissProt
Manually annotated by BRENDA team
at least five isoforms
-
-
Manually annotated by BRENDA team
lemon, sweet and sour
-
-
Manually annotated by BRENDA team
K-12 strains; recombinant overproducing strains
-
-
Manually annotated by BRENDA team
recombinant overproducing strains
-
-
Manually annotated by BRENDA team
strain JE24F+, derived from W3110, uninfected or infected with RNA-phage MS2
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli JE24F+
strain JE24F+, derived from W3110, uninfected or infected with RNA-phage MS2
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
adenylate kinase-deficient patients with chronic hemolytic anemia; isoform 1; patients deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia
SwissProt
Manually annotated by BRENDA team
AK2, fetus
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
heterozygote; post mortem
-
-
Manually annotated by BRENDA team
isoform ecto-adenylate kinase
-
-
Manually annotated by BRENDA team
male adult; post mortem
-
-
Manually annotated by BRENDA team
patients with limbic encephalitis refractory to corticosteroids, IVIg and plasma exchange
-
-
Manually annotated by BRENDA team
post mortem
-
-
Manually annotated by BRENDA team
strain ATCC 29841
UniProt
Manually annotated by BRENDA team
1S2D strain
SwissProt
Manually annotated by BRENDA team
Leishmania donovani 1S2D
1S2D strain
SwissProt
Manually annotated by BRENDA team
strain ATCC 43000D
UniProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
isoform AK1
SwissProt
Manually annotated by BRENDA team
isoform AK2
SwissProt
Manually annotated by BRENDA team
normal or with genetically induced muscular dystrophy
-
-
Manually annotated by BRENDA team
; study on mitochondria during programmed cell death
-
-
Manually annotated by BRENDA team
muscle, two isoforms
-
-
Manually annotated by BRENDA team
rice, two isoforms
-
-
Manually annotated by BRENDA team
slime mold
-
-
Manually annotated by BRENDA team
strains HB3 and Dd2
SwissProt
Manually annotated by BRENDA team
Mre11/Rad50 complex, part of a DNA repair complex
-
-
Manually annotated by BRENDA team
bullfrog
-
-
Manually annotated by BRENDA team
; isoform ecto-adenylate kinase
-
-
Manually annotated by BRENDA team
adult or neonatal
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
Rhodopseudomonas rubrum
-
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
acidic adenylate kinase from pig heart resembles liver mitochondrial enzyme
-
-
Manually annotated by BRENDA team
strain 5068
SwissProt
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
strain 5068
SwissProt
Manually annotated by BRENDA team
bovine parasite
-
-
Manually annotated by BRENDA team
Beneckea, type III
-
-
Manually annotated by BRENDA team
DNA repair complex components Mre11 and Rad50 show adenylate kinase activity when in complex Mre11/Rad50
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
-
adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-ethenoadenosine 5'-triphosphate + AMP
? + ADP
show the reaction diagram
-
not ATP + 1,N6-ethenoadenosine 5'monophosphate
-
ir
adenosine 5'-(3-thio)triphosphate + AMP
adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
show the reaction diagram
-
muscle: reaction at 97% the rate of ATP, liver mitochondria: reaction at 70% the rate of ATP
-
?
ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP
ATP + AMP
show the reaction diagram
-
-
-
?
ADP
ATP + AMP
show the reaction diagram
-
-
-
?
ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP
AMP + ATP
show the reaction diagram
-
-
-
?
ADP
AMP + ATP
show the reaction diagram
-
-
-
r
ADP
AMP + ATP
show the reaction diagram
-
-
-
?
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
Rhodopseudomonas rubrum
-
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrate: CDP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrates: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
-
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrates: IDP, GDP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrates: IDP, GDP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrates: IDP, GDP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrate: UDP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrate: UDP, no substrate: dADP
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
-
no substrates: adenosine tetraphosphate
-
r
ADP + ADP
ATP + AMP
show the reaction diagram
Bacillus subtilis 168
-
-
-
r
ADP + ADP
?
show the reaction diagram
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
ADP + ADP
?
show the reaction diagram
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
ADP + ADP
?
show the reaction diagram
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
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
?
show the reaction diagram
-
involved in energy metabolism
-
-
r
ADP + diphosphate
ATP + phosphate
show the reaction diagram
-
at 0.1% the rate of the natural substrates
-
?
ADP + TDP
AMP + TTP
show the reaction diagram
-
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, rate of TTP synthesis is more than 1000000fold lower than ATP synthesis
-
?
AMP + ATP
ADP
show the reaction diagram
-
-
?
AMP + ATP
ADP
show the reaction diagram
-
-
?
ATP + 7-deazaadenosine 5'-monophosphate
ADP + 7-deazaadenosine 5'-diphosphate
show the reaction diagram
-
i.e. tubercidine monophosphate
-
?
ATP + adenine-9-beta-D-arabinofuranoside 5'-monophosphate
ADP + adenine-9-beta-D-arabinofuranoside 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + adenosine 5'-thiophosphate
?
show the reaction diagram
-
muscle: reaction at 56% the rate of AMP, liver mitochondria: reaction at 95% the rate of AMP
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
Rhodopseudomonas rubrum
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
highly specific
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
best substrates
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
best substrates
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
best substrates
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
best substrates
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are adenosine, 2',3'-AMP or 3',5'-AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
other NMP substrates are very poor acceptors
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
other NMP substrates are very poor acceptors
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are GTP/GMP, TTP/TMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrate of the reverse reaction: CDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrate of the reverse reaction: UDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrate of the reverse reaction: UDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are 3',5'-cAMP, dAMP, 2'-AMP, 3'-AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are GMP, UMP, CMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates of the reverse reaction: adenosine tetraphosphate
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are dGTP/AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are dGTP/AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrate of the reverse reaction: dADP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
less specific for ATP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
less specific for ATP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
specific for ATP, AMP and ADP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrate: ATP alone
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
substrates in decreasing order of activity, in the presence of Mn2+: ATP, 2'-dATP, CTP, GTP, UTP, ITP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/TMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/TMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are adenosine triphosphate 3'-diphosphate, adenosine-5'-(3-thio)triphosphate/adenosine 5'-thiophosphate
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are O1-AMP, epsilon-AMP, 8-bromo-AMP, 2',3'-dialdehyde-AMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates of the reverse reaction: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
substrates in decreasing order of activity, in the presence of Mg2+: ATP, dATP, GTP, ITP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ITP/ADP, ATP/UDP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
-
adenylate kinase isoform G
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
the substrate pair ATP/AMP results in maximal activity
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
ATP is the preferred phosphate donor and AMP is the best phosphate acceptor
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
Bacillus subtilis 168
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
Thermotoga neapolitana 5068
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
Escherichia coli JE24F+
-
-
-
-
ATP + AMP
ADP + ADP
show the reaction diagram
Escherichia coli K12
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
other NMP substrates are very poor acceptors
-
?
ATP + AMP
ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP
show the reaction diagram
-
-
-
r
ATP + AMP
ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP
show the reaction diagram
-
-
?
ATP + AMP
ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP
show the reaction diagram
AMP and dAMP are the preferred substrates, ATP is the best phosphate donor
-
?
ATP + AMP
ADP
show the reaction diagram
-
ATP and AMP are the preferred substrates
-
?
ATP + AMP
AMP + AMP
show the reaction diagram
Leishmania donovani, Leishmania donovani 1S2D
-
-
?
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
?
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
?
ATP + AMP
2 ADP
show the reaction diagram
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
r
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
?
ATP + AMP
2 ADP
show the reaction diagram
-
-
-
?
ATP + AMP + CDP
ADP + AMP + CTP
show the reaction diagram
-
-
-
r
ATP + AMP-3'-diphosphate
?
show the reaction diagram
-
muscle: reaction at 57% the rate of AMP, liver mitochondria: reaction at 86% the rate of AMP
-
-
?
ATP + CDP
ADP + CTP
show the reaction diagram
-
-
nucleoside triphosphate synthesis by beta-phosphoryl transfer from ADP to any bound nucleoside diphosphate
r
ATP + CMP
ADP + ?
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + ?
show the reaction diagram
-
reaction at 10% the rate of AMP
-
?
ATP + CMP
ADP + ?
show the reaction diagram
-
reaction at 1% the rate of AMP
-
?
ATP + CMP
ADP + ?
show the reaction diagram
-
reaction at 1% the rate of AMP
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
adenylate kinase isoform G
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
CMP is a good substrate
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
adenylate kinase 5 domain AK5p1, the relative efficiency of CMP is about 15% compared to AMP
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
phosphorylation of CMP is also detected but to a lesser extend
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
-
-
r
ATP + dAMP
ADP + dADP
show the reaction diagram
-
-
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
2'-dAMP or 3'-dAMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 7% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 10% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 10% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 11% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 46% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
reaction at 30% the rate of AMP
-
-
ATP + dAMP
ADP + dADP
show the reaction diagram
adenylate kinase 5 domain AK5p1
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
-
dAMP is the poorest substrate
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
dCMP is a poor substrate, but preferred over IMP, UMP
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
adenylate kinase 5 domain AK5p1, the relative efficiency of dCMP is about 15% compared to AMP
-
?
ATP + IMP
ADP + IDP
show the reaction diagram
IMP is a poor substrate
-
?
ATP + shikimic acid
ADP + ?
show the reaction diagram
shikimic acid is a good substrate
-
?
ATP + TMP
ADP + TDP
show the reaction diagram
TMP is a good substrate
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
adenylate kinase isoform G
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
UMP is a poor substrate
-
?
CDP + CDP
CTP + CMP
show the reaction diagram
-
-
-
?
CDP + CDP
CTP + CMP
show the reaction diagram
-
poor substrate
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
-
-
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
-
-
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
-
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
15% activity compared to ATP
-
?
CTP + AMP
CDP + ADP
show the reaction diagram
-
adenylate kinase isoform G
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
-
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
-
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at 68% the rate of ATP
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at 12% the rate of ATP
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at 13% the rate of ATP
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at 13% the rate of ATP
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at about 3% the rate of ATP
-
?
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at about 3% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at 25% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
at the same rate as ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
at the same rate as ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at about 50% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at about 50% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at about 50% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at 80% the rate of ATP
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
AMP and dAMP are the preferred substrates, dATP is a good phosphate donor
-
?
dATP + dAMP
dADP
show the reaction diagram
-
-
-
r
dATP + dAMP
dADP + dADP
show the reaction diagram
AMP and dAMP are the preferred substrates
-
?
dCTP + AMP
dCDP + ADP
show the reaction diagram
-
-
-
?
dGTP + AMP
dGDP + ADP
show the reaction diagram
-
-
-
?
dGTP + AMP
dGDP + ADP
show the reaction diagram
-
-
-
?
dTTP + AMP
dTDP + ADP
show the reaction diagram
-
-
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
-
-
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
-
-
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
-
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
-
adenylate kinase isoform G
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
8.4% activity compared to ATP
-
?
GTP + AMP
GDP + ADP
show the reaction diagram
-
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
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
-
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
-
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
reaction at 71% the rate of AMP
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
reaction at 13% the rate of AMP
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
reaction at 5% the rate of AMP
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
reaction at 3% the rate of AMP
-
?
GTP + AMP
GDP
show the reaction diagram
-
-
-
r
GTP + AMP + CDP
GDP + AMP + CTP
show the reaction diagram
-
-
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
-
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
poor substrate
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
9% the rate of ATP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
not ATP/IMP
-
-
ITP + AMP
IDP + ADP
show the reaction diagram
-
not ATP/IMP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
reaction at 10% the rate of ATP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
reaction at 58% the rate of ATP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
8% the rate of ATP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
adenylate kinase isoform G
-
?
TTP + AMP
TDP + ADP
show the reaction diagram
-
-
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
-
-
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
-
-
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
-
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
-
adenylate kinase isoform G
-
?
UTP + AMP
UDP + ADP
show the reaction diagram
1.4% activity compared to ATP
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
-
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
-
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
reaction at 11% the rate of AMP
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
reaction at 12% the rate of AMP
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
reaction at 53% the rate of AMP
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
reaction at 20% the rate of AMP
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
7.2% activity compared to ATP
-
?
additional information
?
-
-
overview: substrate specificity
-
-
-
additional information
?
-
-
the enzyme has broader specificity for NMPs than mammalian enzymes
-
-
-
additional information
?
-
-
ATP + IMP 0.1% activity, ATP + GMP 0.3% activity
-
-
-
additional information
?
-
monophosphates: IMP, GMP, CMP, UMP: activity below 1%
-
-
-
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
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
?
-
-
no substrate: AMP, adenosine
-
-
-
additional information
?
-
-
adenylate kinase activity of the Mre11/Rad50 complex, which is part of a DNA repair complex, promotes DNA-DNA associations
-
-
-
additional information
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
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
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
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
?
-
-
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
?
-
when replacing AMP by GMP, UMP or IMP the measured activity is less than 1%
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
show the reaction diagram
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
ADP + ADP
?
show the reaction diagram
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
ADP + ADP
?
show the reaction diagram
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
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
?
show the reaction diagram
-
involved in energy metabolism
-
-
r
ADP + TDP
AMP + TTP
show the reaction diagram
-
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
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
r
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
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
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
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
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
the adenylate kinase protein preparation contains non-covalently bound ADP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
not
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+; less effective than Mg2+; metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+; metal ion forms complex with di- or trinucleotide; requirement, as good as Mg2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
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+
-
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+
-
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: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
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
Ca2+
the enzyme is slightly activated by Ca2+ (85% relative activity at 5 mM)
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently; requirement
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently; requirement
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
requirement
Co2+
-
requirement
Co2+
-
about 50% as effective as Mg2+; requirement
Co2+
-
about 50% as effective as Mg2+
Co2+
-
the recombinant enzyme can contain Co2+
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+
-
slight activation
Fe2+
-
the recombinant enzyme can contain Fe2+
Fe2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
K+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like K+
K+
the enzyme is highly activated by K+, the optimal concentration is 10 mM
K+
-
maximum stimulation at 100 mM
K+
-
maximum stimulation at 400 mM
K+
maximum stimulation at 200 mM
Li+
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
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+
-
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+
-
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+, Ca2+, Mn2+, Ba2+; 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+, Ca2+, Mn2+, Ba2+; 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+
-
1 mM; requirement
Mg2+
-
requirement
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+; 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+
-
requirement
Mg2+
-
no absolute requirement: 20% of activity in its absence
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; 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+
-
requirement
Mg2+
-
MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
MgADP- is true substrate; requirement
Mg2+
-
MgATP2- is true substrate
Mg2+
-
-
Mg2+
-
-
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+
-
required for activity
Mg2+
-
required for activity
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+
-
required for activity
Mg2+
-
required
Mg2+
the enzyme activity is highly dependent on Mg2+, and the optimal concentration of Mg2+ is 2 mM
Mg2+
-
required for activity
Mg2+
required
Mg2+
-
activity is Mg2+ dependent
Mn2+
-
requirement, about 50% as effective as Mg2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mn2+
-
binding of substrates also takes place in the absence of metal ions; Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mn2+
-
requirement, about 50% as effective as Mg2+
Mn2+
-
requirement, about 25% as effective as Mg2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
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+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like NH4+
NH4+
the enzyme is highly activated by NH4+ (93.6% relative activity at 5 mM)
Zinc
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
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+
-
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+
-
requirement, tightly bound, 0.8 mol Zn2+ per mol protein, atomic absorption spectrophotometry
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+
-
1 mol per mol of enzyme, residual activity after loss
Zn2+
1 mol/mol recombinant enzyme
Zn2+
-
the native enzyme contains 0.03 mol zinc per mole of protein
Zn2+
-
the recombinant enzyme can contain Zn2+
Zn2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
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
additional information
-
no activation by Sr2+
additional information
the enzyme is not activated by Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
above 30 mM, activates below
1,N6-Ethenoadenosine 5'-triphosphate
-
-
3'-O-(4-Benzoyl)benzoyl-ATP
-
-
3-phosphoglyceraldehyde
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: liver enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
muscle enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: liver enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses; strong for muscle enzyme, less effective with dystrophic muscle or liver enzymes
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses; not: mitochondrial enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
not
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: mitochondrial enzyme; only cytosolic
7-deazaadenosine 5'-monophosphate
-
i.e. tubercidine 5'-monophosphate
8-anilino-1-naphthalenesulfonic acid
-
i.e. ANS, isoform N1 binds rapidly, isoform N2 converts to N1 and binds thereafter
8-anilino-1-naphthalenesulfonic acid
-
kinetics
acetyl-CoA
-
-
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
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
adenosine 5'-tetraphosphate
-
weak
adenosine-5'-pentaphosphate
-
weak
ADP
-
in excess, substrate inhibition
Ag+
-
Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
Ag2+
-
predomoninantly muscle type isozymes
AMP
-
product inhibition
AMP
-
above 1 mM; substrate inhibition
AMP
-
substrate inhibition
AMP
-
product inhibition
AMP
-
product inhibition
AMP
-
substrate inhibition
AMP
above 0.007 mM, strong
AMP
-
1 mM, complete inhibition of ADP-dependent ATP production
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
arginine phosphate
-
weak
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
ATP
-
product inhibition
Butanedione
-
-
Ca2+
-
51% inhibition at 1 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
diphosphate
-
reverse reaction
EDTA
-
and other complexing agents
Hg2+
-
strong, not reaction of ADP + ADP
Homologous antibodies
-
-
-
IAA
-
temperature-dependent
IAA
-
plus urea and DTT
iodoacetate
-
temperature-dependent
iodoacetate
-
not
KCl
-
no inhibitory up to 150 mM, 65% residual activity at 700 mM
KCl
-
not inhibitory up to 150 mM, 65% residual activity at 700 mM
Methylmercury nitrate
-
-
Mg2+
-
at high concentrations; required for enzyme activity at low concentrations
Mg2+
-
above 0.5 mM
Mg2+
-
at a high Mg:ATP ratio
N-ethylmaleimide
-
not
N-ethylmaleimide
-
weak
N-ethylmaleimide
-
-
oleic acid
-
-
p-Chloromercuriphenylsulfonate
-
-
p-Hydroxymercuribenzene sulfonic acid
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
strong, reversible by GSH or cysteine
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,P4-diadenosine tetraphosphate
-
-
P1,P4-diadenosine tetraphosphate
-
i.e. P1,P4-bis(5'-adenosyl)-tetraphosphate, transition state analogue, kinetics
P1,P4-diadenosine tetraphosphate
-
weak
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
P1,P5-di(adenosine-5') pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
1 M
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
50% inhibition at 0.00041 mM, reactivation by 1 mM ADP if concentration of inhibitior is below 0.001 mM. No inhibition if 1 mM ADP is present; 50% inhibition at 0.00053 mM, recombinant enzyme; completely inhibits reactivation of flagella. 1 mM ADP prevents inhibition
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to Rad50 phosphoryl transfer reaction but not to ATP hydrolysis
P1,P5-di(adenosine-5')pentaphosphate
-
completely abolishes adenylate kinase activity but does not affect ATPase activity
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to Rad50 phosphoryl transfer reaction but not to ATP hydrolysis. Inhibitor blocks DNA tethering in vitro and in cell-free extracts
P1,P5-di(adenosine-5')pentaphosphate
-
; decreases the rate of decomposition of ADP and inhibits the formation of ATP
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P5-di(adenosine-5')pentaphosphate
-
inhibition of adenylate kinase prevents the stimulatory effect of AMP on K/ATP channels
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
50% inhibition at 50 mM, whether assayed in the direction of ATP formation from ADP or of ATP conversion to ADP
P1,P5-di(adenosine-5')pentaphosphate
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
strong
P1,P5-diadenosine 5'-pentaphosphate
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
specific inhibitor
P1,P5-diadenosine 5'-pentaphosphate
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
i.e. AP5A or P1,P5-bis(5'-adenosyl)-pentaphosphate, bisubstrate analogue; kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
above 100 nM; strong
P1,P5-diadenosine 5'-pentaphosphate
-
competitive for formation of ADP, noncompetitive for formation of ATP
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5-pentaphosphate
adenylate kinase-specific inhibitor, potent inhibitor of CINAP
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
sulfhydryl reagents
-
-
sulfur
-
elemental sulfur, reversible by dithiothreitol, muscle, not liver isozyme
suramin
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
Urea
-
plus dithiothreitol and IAA
uridine adenosine tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
Mg2+
-
strong inhibition in catalyzed reaction is observed when Mg2+concentration is in excess
additional information
-
effect of varios intermediary metabolites; no inhibition by K+, Na+, NH4+, AsO2, citrate, NADH, fructose 6-phosphate, 2-phosphoglyceraldehyde
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
additional information
-
-
-
additional information
-
not inhibitory: P1,P2-di(adenosine-5')diphosphate, P1,P3-di(adenosine-5') triphosphate, triphosphate, tetrahexaphosphate, tetrametaphosphate, hexametaphosphate
-
additional information
-
not inhibitory: citrate
-
additional information
-
not inhibitory: citrate
-
additional information
not inhibitory: EDTA 10mM
-
additional information
not inhibitory: atractyloside, chloroquine, primaquine, artemisinine, mefloquine
-
additional information
-
after 2 h from heat-shock, when cell viability remains unaffected, the rate of ADP/ATP exchange due to adenine nucleotide translocator activity, and the activites of adenylate kinase and nucleoside diphosphate kinase are inhibited in a non-competitive like manner. Externally added ascorbate partially prevents inhibition
-
additional information
-
no inhibition by dipyramidole, flufenamic acid, pyridoxal-5-phosphate-6-azophenyl-2,4-disulfonic acid tetrasodium or p-nitrophenylphosphate; not inhibitory: dipyridamole, flufenamic acid, pyridoxal-5-phosphate-6-azophenyl-2',4'-disulphonic acid tetrasodium, and p-nitrophenylphosphate
-
additional information
not inhibited by N-ethylmaleimide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
inhibitory above 30 mM, activates below
2-mercaptoethanol
-
activation
2-oxoglutarate
-
activation
ADP
-
induction of cellular ATP production via adenylate kinase resulting in regulation of ADP-dependent endocytosis of high-density lipoprotein
alanine
-
activation
AMP
-
adenylate kinase activation by ATP and AMP stimulates K/ATP channel activity and this stimulation is abolished by adenylate kinase inhibitors
ATP
-
adenylate kinase activation by ATP and AMP stimulates K/ATP channel activity and this stimulation is abolished by adenylate kinase inhibitors
CDP
-
activation
cis-aconitate
-
activation
citrate
-
not
citrate
-
activation
dithiothreitol
-
activation
dithiothreitol
-
not
fumarate
-
activation
GDP
-
activation
Isocitrate
-
activation
KCl
-
activation
L-cysteine
-
activation
L-cysteine
-
activation
L-histidine
-
activation
NaCl
-
activation, 0.5-0.8 M
NH4Cl
-
activation
Prostaglandins
-
activation
-
sulfhydryl compounds
-
requirement
TDP
-
activation
Thermolysin
-
significant increase of specific activity (1.5-fold) after a short (60 min, 50 C) proteolytic treatment with thermolysin
-
threonine
-
activation
UDP
-
activation
Urea
-
up to 1 M, 60% increase in activity
malate
-
activation
additional information
-
no activation by GTP, CTP, UTP, TTP, 2'-dGTP, 2'-dCTP, 2'-dATP, GMP, CMP, UMP, TMP, IMP, 2'-dAMP or 3',5'-cAMP; no activation by succinate or oxaloacetate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
2'-dAMP
-
cosubstrate ATP, pH 7.4, 27C
0.73
7-deazaadenosine 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27C
1.3 - 1.37
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27C
0.003
ADP
-
cosubstrate MgADP-, pH 7.8, 25C
0.028
ADP
-
pH 8.1
0.046
ADP
-
25C, pH 8.1, isoform N2
0.05
ADP
-
-
0.088
ADP
-
-
0.11
ADP
-
cosubstrate ATP, pH 8.5
0.11
ADP
-
25C, pH 8.0
0.128
ADP
-
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.165
ADP
-
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.23
ADP
pH 7.6, 16C, recombinant enzyme
0.24 - 0.27
ADP
-
-
0.24 - 0.27
ADP
-
25C, pH 7.6
0.247
ADP
-
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.32
ADP
pH 7.6, 16C; pH 7.6, 16C, enzyme from sperm flagellum; pH 7.6, isolated flagella
0.32
ADP
-
enzyme from sperm flagella, pH 7.6, 16C
0.34 - 0.35
ADP
-
25C, pH 8.0
0.34 - 0.35
ADP
-
cosubstrate ATP
0.34 - 0.35
ADP
-
pH 8.7, 25C
0.45 - 0.55
ADP
-
30C, pH 7.4
0.45 - 0.55
ADP
-
pH 8.5
0.65 - 0.7
ADP
-
-
0.65 - 0.7
ADP
-
70C
0.65 - 0.7
ADP
-
-
0.69
ADP
pH 7.6, 16C, enzyme from embryonic cilia
0.69
ADP
-
enzyme from cilia, pH 7.6, 16C
1.3
ADP
-
90C, pH is not specified in the publication
2.2
ADP
in 100 mM TrisHCl (pH 7.5), 20 mM glucose, 5 mM MgCl2, 10 mM KCl, 2 mM dithiothreitol, at 37C
16.8
ADP
-
37C, pH 7.0
0.03
ADP3-
-
pH 8, 25C
0.09 - 0.092
ADP3-
-
pH 7.5, 30C
0.09 - 0.092
ADP3-
-
ATP production; pH 8.7, 25C
0.09 - 0.092
ADP3-
-
ADP, 30C
0.09 - 0.092
ADP3-
-
25C, pH 8.0; ATP production
0.0014
AMP
-
recombinant adenylate kinase 4, using GTP as cosubstrate
0.0032
AMP
-
-
0.0053
AMP
-
recombinant adenylate kinase 4, using ATP as cosubstrate
0.00959
AMP
at 30C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.011
AMP
-
wild-type, pH 7.2, 27C
0.013
AMP
-
mutant Q199R, pH 7.2, 27C
0.016
AMP
-
wild-type, pH 7.2, 35C
0.0214
AMP
at 22C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.0216
AMP
at 40C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.024
AMP
-
mutant Q199R, pH 7.2, 35C
0.024
AMP
at 30C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.026
AMP
-
wild-type, pH 7.2, 45C
0.037
AMP
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.0372
AMP
at 40C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.038 - 0.04
AMP
-
pH 7.5, 25C, ADP production
0.038 - 0.04
AMP
-
pH 7.4, 27C
0.038 - 0.04
AMP
-
cosubstrate ATP, 30C
0.04
AMP
-
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.0409
AMP
30C, pH 7.4
0.046
AMP
-
mutant Q199R, pH 7.2, 45C
0.046
AMP
-
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.048
AMP
-
wild-type, pH 7.2, 55C
0.048
AMP
-
in 50 mM Tris-HCl pH 7.6, 5 mM MgCl2, at 37C
0.05
AMP
pH 6.0 and pH 7.4
0.05547
AMP
at 60C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.069
AMP
-
cosubstrate MgATP, pH 7.8, 25C
0.07
AMP
mutant G40R, 37C; mutant G40R, 37C, pH 8.0
0.07
AMP
-
wild-type, pH 7.2, 60C
0.071
AMP
-
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.07389
AMP
at 50C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.076 - 0.083
AMP
-
-
0.076 - 0.083
AMP
-
37C
0.076 - 0.083
AMP
-
25C, pH 8.0
0.08
AMP
mutant G64R, 37C; mutant G64R, 37C, pH 8.0
0.081
AMP
-
25C, pH 8.1, isoform N1
0.094
AMP
-
mutant Q199R, pH 7.2, 55C
0.11
AMP
-
mutant Q199R, pH 7.2, 60C
0.114 - 0.13
AMP
-
-
0.114 - 0.13
AMP
-
-
0.114 - 0.13
AMP
-
pH 8.5
0.114 - 0.13
AMP
-
-
0.12
AMP
-
pH 7.5
0.172
AMP
adenylate kinase 5 domain AK5p1, with ATP as phosphate donor
0.18
AMP
-
-
0.192
AMP
-
-
0.244
AMP
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.29
AMP
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25C
0.32
AMP
-
25C, pH 8.0
0.38
AMP
wild-type, 37C; wild-type, 37C, pH 8.0
0.5 - 0.6
AMP
-
-
0.5 - 0.6
AMP
-
cosubstrate ATP, 70C
0.547
AMP
-
25C, pH 8.1, isoform N2
1.01
AMP
mutant Y164C, 37C; mutant Y164C, 37C, pH 8.0
1.039
AMP
-
25C, pH 8.1, isoform N1
1.1
AMP
-
90C, pH is not specified in the publication
1.17
AMP
-
-
1.3 - 1.37
AMP
-
90C
1.6
AMP
mutant R11128W, 37C, pH 8.0; mutant R128W, 37C
1.7
AMP
mutant D140del, 37C; mutant D140del, 37C, pH 8.0
1.9
AMP
-
37C, pH 7.0
0.000063
ATP
-
isoenzyme AK1, membrane protein fraction
0.000141
ATP
-
isoenzyme AK1b, cytosolic protein fraction
0.00018
ATP
-
-
0.00073
ATP
-
isoenzyme AK1b, membrane protein fraction
0.000998
ATP
-
isoenzyme AK1, cytosolic protein fraction
0.0018
ATP
at 30C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 6 5mM KCl
0.002
ATP
at 22C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl; at 40C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.00537
ATP
at 30C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.013
ATP
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.01659
ATP
at 40C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.034
ATP
-
Zn2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.036 - 0.037
ATP
-
ADP, 37C
0.044
ATP
-
-
0.045
ATP
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.048 - 0.051
ATP
-
pH 7.4, 27C
0.048 - 0.051
ATP
-
cosubstrate AMP, 30C
0.049
ATP
-
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.0494
ATP
30C, pH 7.4
0.06
ATP
mutant G40R, 37C; mutant G40R, 37C, pH 8.0
0.067
ATP
-
30C, pH 7.4
0.075
ATP
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25C
0.076
ATP
-
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.084
ATP
-
cosubstrate 2'-dAMP, 27C, pH 7.4
0.093
ATP
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.09471
ATP
at 50C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.13
ATP
wild-type, 37C; wild-type, 37C, pH 8.0
0.1349
ATP
at 60C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.195 - 0.203
ATP
-
-
0.195 - 0.203
ATP
-
-
0.27 - 0.3
ATP
-
-
0.27 - 0.3
ATP
-
25C, pH 8.0
0.27 - 0.3
ATP
-
cosubstrate 3'-dAMP, pH 7.4, 27C
0.272
ATP
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
0.38
ATP
mutant G64R, 37C; mutant G64R, 37C, pH 8.0
0.4
ATP
mutant D140del, 37C; mutant D140del, 37C, pH 8.0
0.5
ATP
mutant Y164C, 37C; mutant Y164C, 37C, pH 8.0
0.95
ATP
-
-
1.03
ATP
mutant R11128W, 37C, pH 8.0; mutant R128W, 37C
1.1
ATP
-
90C, pH is not specified in the publication
7
ATP
-
37C, pH 7.0
0.00017
CMP
-
-
0.507
dAMP
-
recombinant adenylate kinase 4, using ATP as cosubstrate
2
dAMP
Km above 2.0 mM, adenylate kinase 5 domain AK5p1, with ATP as phosphate donor
0.006
MgADP-
-
cosubstrate ADP, pH 7.8, 25C
0.15
MgADP-
-
-
0.15
MgADP-
-
cosubstrate AMP
0.025
MgATP2-
-
cosubstrate AMP, pH 7.8, 25C
0.06
MgATP2-
-
pH 7.5
0.072
MgATP2-
-
25C, pH 8.1, isoform N2
0.13
MgATP2-
-
25C, pH 8.1, isoform N1
0.23
MgATP2-
-
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10C to 50C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
783
ADP
Homo sapiens
-
-
0.015
AMP
Bacillus subtilis
-
mutant Q199R, pH 7.2, 27C
0.035
AMP
Bacillus subtilis
-
mutant Q199R, pH 7.2, 35C; wild-type, pH 7.2, 27C
0.053
AMP
Bacillus subtilis
-
wild-type, pH 7.2, 35C
0.06
AMP
Bacillus subtilis
-
mutant Q199R, pH 7.2, 45C
0.073
AMP
Bacillus subtilis
-
wild-type, pH 7.2, 45C
0.1
AMP
Bacillus subtilis
-
wild-type, pH 7.2, 55C
0.13
AMP
Bacillus subtilis
-
mutant Q199R, pH 7.2, 55C
0.135
AMP
Bacillus subtilis
-
wild-type, pH 7.2, 60C
0.16
AMP
Homo sapiens
P00568
mutant G40R, 37C; mutant G40R, 37C, pH 8.0
0.19
AMP
Bacillus subtilis
-
mutant Q199R, pH 7.2, 60C
0.21
AMP
Homo sapiens
P00568
mutant D140del, 37C; mutant D140del, 37C, pH 8.0
0.57
AMP
Homo sapiens
P00568
mutant Y164C, 37C, pH 8.0
0.63
AMP
Homo sapiens
P00568
mutant G64R, 37C; mutant G64R, 37C, pH 8.0
8.3
AMP
Schistosoma mansoni
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
50
AMP
Schistosoma mansoni
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
55.3
AMP
Homo sapiens
P00568
mutant R11128W, 37C, pH 8.0; mutant R128W, 37C
234.4
AMP
Homo sapiens
P00568
mutant Y164C, 37C
842
AMP
Homo sapiens
P00568
wild-type, 37C, pH 8.0
842.3
AMP
Homo sapiens
P00568
wild-type, 37C
0.0037
ATP
Homo sapiens
Q9Y3D8
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.0063
ATP
Homo sapiens
Q9Y3D8
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.1
ATP
Homo sapiens
P00568
mutant R11128W, 37C, pH 8.0
0.11
ATP
Homo sapiens
P00568
mutant G40R, 37C; mutant G40R, 37C, pH 8.0
0.17
ATP
Homo sapiens
P00568
mutant D140del, 37C; mutant D140del, 37C, pH 8.0
0.65
ATP
Homo sapiens
P00568
mutant G64R, 37C; mutant G64R, 37C, pH 8.0
5
ATP
Schistosoma mansoni
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
5.4
ATP
Plasmodium falciparum
Q14EL6
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25C
25
ATP
Schistosoma mansoni
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
48.32
ATP
Homo sapiens
P00568
mutant R128W, 37C
152
ATP
Homo sapiens
-
allelozyme AK1*2
170
ATP
Sulfolobus acidocaldarius
-
70C, pH is not specified in the publication
220.3
ATP
Homo sapiens
P00568
mutant Y164C, 37C
325
ATP
Vibrio natriegens
-
-
417
ATP
Oryctolagus cuniculus
-
25C
683
ATP
Homo sapiens
-
-
879
ATP
Homo sapiens
P00568
wild-type, 37C, pH 8.0
879.5
ATP
Homo sapiens
P00568
wild-type, 37C
additional information
additional information
Oryctolagus cuniculus
-
26300 for formation of ATP at 30C, 28000 for formation of ATP at 25C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4500
AMP
Schistosoma mansoni
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
30
4900
AMP
Schistosoma mansoni
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
30
2600
ATP
Schistosoma mansoni
-
isoform ADK2, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
4
11000
ATP
Schistosoma mansoni
-
isoform ADK1, in 20 mM Tris-HCl (pH 7.4), 150 mM NaCl and 5 mM 2-mercaptoethanol, temperature not specified in the publication
4
39000
ATP
Homo sapiens
Q9Y3D8
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
4
140000
ATP
Homo sapiens
Q9Y3D8
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
4
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
7-deazaadenosine 5'-monophosphate
-
-
0.55
8-Bromo-AMP
-
-
0.91
ADP
-
pH 8.1
3.3
AMP
-
pH 7.5
0.00038
P1,P5-di(adenosine-5')pentaphosphate
pH 6
0.000002
P1,P5-diadenosine 5'-pentaphosphate
-
-
0.0023
P1,P5-diadenosine 5'-pentaphosphate
-
-
0.00002703
P1,P5-diadenosine 5-pentaphosphate
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
P1,P5-(diadenosine-5')-pentaphosphate
Plasmodium falciparum
Q14EL6
-
0.00041
P1,P5-di(adenosine-5')pentaphosphate
Strongylocentrotus purpuratus
A2T1M5
pH 7.6, 16C
0.00053
P1,P5-di(adenosine-5')pentaphosphate
Strongylocentrotus purpuratus
-
pH 7.6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.011
mutant enzyme CINAP H79G, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
0.018
wild type enzyme CINAP, in 100 mM Tris-HCl, pH 7.5, 60 mM KCl, temperature not specified in the publication
10
recombinant enzyme, in 110 mM TEA-HCl, pH 7.6, at 25C
14
-
substrate: ATP, pH and temperature not specified in the publication
32
-
pH 8.7, 25C, ATP production
56
substrate: ATP, pH and temperature not specified in the publication
60
-
isozyme II
76.7 - 79.3
-
25C, pH 8.0
81
-
substrate: ATP, pH and temperature not specified in the publication
89
-
substrate: ATP, pH and temperature not specified in the publication
129
-
mutant S129F
225 - 250
-
liver, 30C, pH 8.1
230
-
liver, pH 8.0, 30C
250
-
mutant P87S
280
-
30C, pH 7.4
350 - 400
-
-
420
-
allelozyme AK1*2
1000
-
liver isozyme III
1062
-
liver, mitochondria
1400 - 1600
-
muscle, 30C, pH 8.1
1450
-
30C, pH 7.4
1480
-
allelozyme AK1*1
1550
-
-
1560
-
apoenzyme, pH 7.4, 30C
1600 - 1700
-
muscle, 30C, pH 8.1
1600 - 1700
-
-
1600 - 1700
-
liver enzyme, pH 7.4, 30C
1600 - 1700
-
muscle enzyme, pH 8.1
1640
-
ATP formation, pH 7.4, 30C
1700 - 1800
-
muscle, 30C, pH 8.1
1810
-
muscle
1900
-
muscle enzyme, pH 7.4, 30C
1920
-
muscle
1920
-
25C, pH 8.0
1980
-
fully zinc-substitued form, pH 7.4, 30C
2000
wild-type, 37C
2020
-
native form, pH 7.4, 30C
2170
-
fully cobalt-substitued form, pH 7.4, 30C
2244
-
muscle, pH 8.0, 30C
3200
-
-
3200
-
25C, pH 8.0
additional information
-
-
additional information
-
kinetics
additional information
Vmax 1130 30C
additional information
Vmax 0.00018 pH 8
additional information
-
Vmax 77 AMP/ATP; Vmax 78 CMP/CTP
additional information
Vmax 75 1 mM at pH 6.0 and 25C
additional information
-
Vmax 0.955 AMP variable; Vmax 0.982 ATP variable
additional information
-
adenylate kinase-like protein 1 is able to catalyze the conversion of ATP and AMP in vitro with a specific activity of about 3 milliunits/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
-
AMP + ATP, 70C
5.3
-
ATP formation
5.8
-
AMP + ATP, acidic heart enzyme
5.8
-
-
6
-
AMP + ATP, 70C
6
-
ADP formation
6 - 7.5
-
liver enzyme
6 - 9
-
broad, muscle enzyme
7
-
ADP + ADP, acidic heart enzyme
7 - 7.6
-
broad
7 - 8
-
muscle enzyme
7.4
-
AMP + ATP
7.4
-
AMP + ATP
7.4 - 8.6
-
broad
7.9
-
ADP + ADP
8
-
ADP + ADP
8.1
-
recombinant full-length protein
8.2
-
AMP + ATP
8.2
-
ADP + ADP
8.7
-
ADP + ADP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7
-
about half-maximal activity at pH 3.5 and about 70% of maximal activity at pH 7, ADP + ADP, 70C
4 - 7.5
-
about half-maximal activity at pH 4 and about 70% of maximal activity at pH 7.5, AMP + ATP, 70C
5 - 10
-
less than 20% of maximal activity at pH 5, 5.5, 6 and pH 9.5 and 10, about half-maximal activity at pH 6.9 and 8.4
5 - 7.5
-
about half-maximal activity at pH 5 and 7.5, AMP + ATP, acidic heart enzyme
5.1 - 11
-
about half-maximal activity at pH 5.1 and pH 11, muscle enzyme
5.5 - 10
-
about half-maximal activity at pH 5.5 and about 60% of maximal activity at pH 10, AMP + ATP
5.6 - 10.5
-
about half-maximal activity at pH 5.6 and about 60% of maximal activity at pH 10.5
5.8 - 6.5
-
direction of ADP formation
6 - 10
-
about half-maximal activity at pH 6 and 10, AMP + ATP
6 - 10
-
enzyme shows similar activity over a pH range from 6 to 10
6 - 11
-
about half-maximal activity at pH 6 and 11, ADP + ADP
6 - 8.5
-
about half-maximal activity at pH 6 and 8.5, ADP + ADP, acidic heart enzyme
6.5 - 8.2
-
about half-maximal activity at pH 6.5 and 8.2
6.9 - 8.4
-
about half-maximal activity at pH 6.9 and 8.4
7
more than 70% active
7.5 - 9
-
direction of ATP formation
8 - 10
-
about half-maximal activity at pH 7.5
8.5
more than 70% active
8.5 - 11.5
-
about half-maximal activity at pH 8.5 and 11.5, ADP + ADP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
highly active at 30C
32
-
temperature optimum of Fe2+-containing adenylate kinase
36
-
temperature optima of Zn2+- and Co2+-containing adenylate kinase
37
-
assay at
37
-
wild-type enzyme
45
-
mutant enzyme J36V
50
-
around 50C
53
-
mutant enzyme V160J
72
-
mutant enzyme V36J
75
-
mutant enzyme J160V
80
-
long term incubation
80
-
wild-type enzyme
83
-
wild-type enzyme
90
-
incubation time 60 s
additional information
-
effect of temperature on initial velocity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
-
25C: about 85% of maximal activity, 60C: about 60% of maximal activity, wilde-type enzyme
30 - 60
excellent activity over a broad temperature range of 30-60C
60 - 90
-
60C: about 50% of amximal activity, 90C: about 89% of maximal activity
70 - 95
-
about half-maximal activity at 70C and about 75% of maximal activity at 95C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
-
isoelectric focusing
4.45
-
isoelectric focusing
4.5
-
isoelectric focusing
4.7 - 4.8
-
isoelectric focusing
4.9
-
calculated from amino acid sequence
5.7
-
isoelectric focusing
6.1
-
muscle enzyme
6.7
-
isoelectric focusing
7
-
muscle enzyme
7.5
-
liver type enzymes
7.5
estimated from amino acid sequence
8.1
-
liver enzyme
8.9
; calculated
8.9
-
calculated from amino acid sequence
9
-
isozyme AKalpha, isoelectric focusing
9.3
-
mitochondrial enzyme, isoelectric focusing
9.6
-
liver, isoelectric focusing
10.1
-
cytosolic enzyme
10.1
-
muscle enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
muscle isozyme
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
-
isolated embryonic cilia. A 130000 Dalton isoform is responsible for 93% of nonmitochondrial ATP regeneration from ADP in cilia. Presence of at least one additional adenylate kinase isoform
Manually annotated by BRENDA team
-
vascular endothelial cells
Manually annotated by BRENDA team
most of protein is tightly bound to the axoneme
Manually annotated by BRENDA team
-
muscle isozyme
Manually annotated by BRENDA team
-
isoform AK2
Manually annotated by BRENDA team
-
in primary culture
Manually annotated by BRENDA team
-
; hippocampal slices, presence of an ecto-adenylate kinase
Manually annotated by BRENDA team
-
adenylate kinase 2 is specifically expressed in the stria vascularis region of the inner ear
Manually annotated by BRENDA team
-
liver isozyme
Manually annotated by BRENDA team
-
isoform AK2
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
breast muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
isoform AK2, skeletal muscle
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
-
cytosolic isoforms AK1 and AK5 are expressed in human islets and INS-1 cells. Elevated concentrations of glucose inhibit AK1 expression
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
Leishmania donovani 1S2D
-
-
-
Manually annotated by BRENDA team
-
in contrast to decreased levels of pyruvate kinase, enolase and phosphofructokinase, the mitochondrial ATP synthase, succinate dehydrogenase, malate dehydrogenase, isocitrate dehydrogenase and adenylate kinase are increased in senescent fibres
Manually annotated by BRENDA team
-
neonatal rats
Manually annotated by BRENDA team
-
sperm flagellum. 31% of the nonmitochondrial ATP regeneration are due to the 130000 Dalton adenylate kinase isozyme and 69% due to the flagellar creatine kinase
Manually annotated by BRENDA team
expression is upregulated during late spermiogenesis when the flagellum is being assembled; mRNA is present at low but relatively equivalent levels in pachytene spermatocytes, round spermatids, and condensing spermatids
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
-
; non-photosynthetic cell
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
moderate expression
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
high activities in tissues where turnover of energy from adenine nucleotides is great, e. g. muscle; rabbit and human carry a minimum of 2 sets of isozymes within an individual: one set in muscle, erythrocytes, brain and another in liver, kidney and spleen; tissue distribution
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
high activities in tissues where turnover of energy from adenine nucleotides is great, e. g. muscle; rabbit and human carry a minimum of 2 sets of isozymes within an individual: one set in muscle, erythrocytes, brain and another in liver, kidney and spleen; tissue distribution
Manually annotated by BRENDA team
additional information
-
high activities in tissues where turnover of energy from adenine nucleotides is great, e. g. muscle; tissue distribution
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
cell-free synthesis in mRNA-dependent rabbit reticulocyte lysate system
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
present in all tissues tested
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoenzyme AK1b
-
Manually annotated by BRENDA team
-
isolated embryonic cilia. A 130000 Dalton isoform is responsible for 93% of nonmitochondrial ATP regeneration from ADP in cilia. Presence of at least one additional adenylate kinase isoform
Manually annotated by BRENDA team
-
cytosolic and mitochondrial kinases are distinct isozymes
Manually annotated by BRENDA team
-
cytosolic and mitochondrial kinases are distinct isozymes
Manually annotated by BRENDA team
-
breast muscle enzyme
Manually annotated by BRENDA team
-
isoenzyme AK1
Manually annotated by BRENDA team
; isoform adenylate kinase 1
Manually annotated by BRENDA team
-
isoform AK1 and adenylate kinase-like protein 1
Manually annotated by BRENDA team
-
extracellular activity is less than 1% of total activity and due to leaking from leaving cells or to dying cells
-
Manually annotated by BRENDA team
-
cytoplasmic adenylate kinase 1 is secreted from myotubes but not from myoblasts
-
Manually annotated by BRENDA team
localizes along the entire flagellum, tightly bound to the axoneme. Enzyme contributes 31% of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme
-
Manually annotated by BRENDA team
-
sperm flagellum. 31% of the nonmitochondrial ATP regeneration are due to the 130000 Dalton adenylate kinase isozyme and 69% due to the flagellar creatine kinase
-
Manually annotated by BRENDA team
-
adenylate kinase isoform D
Manually annotated by BRENDA team
-
extracellular activity is less than 1% of total activity and due to leaking from leaving cells or to dying cells
Manually annotated by BRENDA team
-
N-myristoylation is required to target isoform AK2 to the parasitophorous vacuole membrane
Manually annotated by BRENDA team
-
cytosolic and mitochondrial kinases are distinct isozymes; intermembrane space
Manually annotated by BRENDA team
-
cytosolic and mitochondrial kinases are distinct isozymes
Manually annotated by BRENDA team
-
intermembrane space
Manually annotated by BRENDA team
-
after 2 h from heat shock, rate of ADT/ATP exchange by adenine nucleotide translocator activity, adenylate kinase activity and nucleoside diphosphate kinase EC 2.7.4.6 are inhibitied in a non-competitive-like manner. Externally added ascorbate prevents the inhibition
Manually annotated by BRENDA team
most highly expressed isoform AK1
Manually annotated by BRENDA team
localized in the mitochondrial intermembrane space
Manually annotated by BRENDA team
-
nucleolar localization is dependent on nutrient availability and active transcription and ribosome assembly and is lost upon oxidative stress
Manually annotated by BRENDA team
predominant localization
Manually annotated by BRENDA team
-
predominant nuclear localization
Manually annotated by BRENDA team
-
decreased expression in growing tubers leads to increased rates of respiratory oxygen consumption and increased carbon fluxes into starch. Increased rates of starch synthesis are accompanied by post-translational redox-activation of ADP-glucose diphosphorylase, while there are no substantial changes in metabolic intermediates or sugar levels
Manually annotated by BRENDA team
-
; presence of an ecto-adenylate kinase
-
Manually annotated by BRENDA team
additional information
-
particle-associated; subcellular distribution of 4 rat isozymes
-
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
additional information
-
stroma-associated
-
Manually annotated by BRENDA team
additional information
localizes to the mitochondrial sheath in sperm midpiece; localizes to the sodium dodecyl sulfate insoluble sperm tail fraction
-
Manually annotated by BRENDA team
additional information
isoforms AMK1 to AMK5 are much higher expressed than AMK6, while AMK7 is at the detection limit
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Methanococcus maripaludis (strain S2 / LL)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
-
muscle, sedimentation and diffusion
642556
21000
-
eye lens
642558
21000
-
muscle, sedimentation and diffusion
642558
21000
-
electrospray ionization mass spectroscopy
642619
21200
-
muscle, sedimentation equilibrium
642573
21300
-
-
642558
21300
-
muscle
642558
21300
-
isozyme AKalpha, sedimentation equilibrium; sedimentation equilibrium
642567
21300
-
sedimentation equilibrium
642603
21500
-
liver mitochondria
642558
21500
-
-
642558
21500
-
muscle, gel filtration
642564
21700
-
amino acid analysis
642564
22000
-
sedimentation equilibrium
642560
22000
calculated from amino acid sequence
642575
22000
-
gel filtration
642593
22000
-
adenylate kinase 1, SDS-PAGE
705850
22500
-
isozyme AKalpha, gel filtration
642567
22600
-
titration of 2 SH-groups
642564
22940
-
sedimentation equilibrium
642585
23000
-
-
642558
23000
-
isozyme III, at concentrations above 3 mg/ml, dimers and trimers of MW 46000 and 68000 are formed
642558
23000
-
gel filtration
642563
23000
-
muscle, gel filtration
642601
23500
-
gel filtration
642588
23560
-
calculated from nucleotide sequence
642584
24000
-
gel filtration
662337
24100
-
calculated from nucleotide sequence
642587
24140
-
calculated from nucleotide sequence
642586
24700
-
gel filtration
661349
24700
-
estimated from SDS-PAGE
704057
25000
-
and 50000, gel filtration and non-reducing SDS-PAGE
691028
25000
-
SDS-PAGE
705851
25200
-
liver, sedimentation equilibrium
642559
25400
-
sedimentation equilibrium
642560
25600
-
liver, sedimentation equilibrium
642573
26000
-
gel filtration
642577
26000
calculated from nucleotide sequence
661631
26000
-
gel filtration
693492
26000
-
adenylate kinase 2, SDS-PAGE
705850
26350
-
calculated from amino acid analysis
642559
26900
-
acidic isozyme, PAGE
642569
27000
-
gel filtration
642600
27000
SDS-PAGE
703297
27500
-
gel filtration
642574
27600
calculated without His-tag
662798
29000
-
-
642576
29000
-
gel filtration
642580
29000
gel filtration
660952
30000
-
gel filtration
642624
31000
-
liver, gel filtration
642601
31500
-
gel filtration
642592
32100
Rhodopseudomonas rubrum
-
gel filtration
642581
32500
estimated from amino acid sequence
705595
33500
-
gel filtration
642581
34000
estimated from SDS-PAGE
705595
34400
-
gel filtration
642581
40000
-
sucrose density gradient centrifugation
642578
41000
-
-
642558
46000 - 49000
-
isozyme II
642558
46000 - 49000
-
analytical ultracentrifugation
642602
50000
-
and 25000, gel filtration and non-reducing SDS-PAGE
691028
52000
-
gel filtration
642582
53000
-
SDS-PAGE, fused with the GST tag the recombinant protein has a size of about 53000 Da
704047
63000
gel filtration, sedimentation analysis
642614
additional information
-
a great deal of homology and some distinct differences between liver and muscle type enzymes of different organisms; comparison of amino acid composition of different sources
642560
additional information
-
comparison of amino acid composition of different sources
642572
additional information
-
molecular weights of enzymes from different organisms
642589
additional information
-
amino acid composition
642595
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 24000, SDS-PAGE
?
-
x * 25600, SDS-PAGE
?
x * 22000, SDS-PAGE; x * 28000, SDS-PAGE
?
x * 21000-23000, SDS-PAGE
?
x * 22000, SDS-PAGE, x * 21635, calculated
?
x * 130000, full-length enzyme, 21000, recombinant expression of catalytic domain 1 or 3, 22000, recombinant expression of catalytic domain 2, SDS-PAGE
?
-
x * 130000, SDS-PAGE
?
-
x * 21000, SDS-PAGE; x * 21110, calculated from sequence
?
-
x * 27000, calculated from amino acid sequence; x * 33000, His-tagged enzyme, SDS-PAGE
?
-
x * 25000, adenylate kinase-like protein 1, SDS-PAGE
?
-
x * 48500, calculated from amino acid sequence
?
x * 26700, His12-tagged enzyme ADK1, estimated from SDS-PAGE
?
-
x * 22600, calculated from amino acid sequence; x * 27000-28000, SDS-PAGE
?
-
x * 25000, SDS-PAGE
?
-
x * 25000 (approximately), SDS-PAGE
?
-
x * 25000, SDS-PAGE
?
-
x * 25000 (approximately), SDS-PAGE
?
x * 25000 (approximately), SDS-PAGE
?
-
x * 25000 (approximately), SDS-PAGE
-
dimer
-
isozyme III, at concentrations above 3 mg/ml, dimers and trimers of MW 46000 and 68000 are formed
dimer
-
2 * 23500, SDS-PAGE
dimer
-
2 * 22000 isoenzyme AK1, SDS-PAGE; 2 * 23000 isoenzyme AK1b, SDS-PAGE
dimer
-
2 * 21170, calculated from sequence
dimer
-
and monomer, 2 * 27000, SDS-PAGE
dimer
-
cobalt-bound enzyme, X-ray crystallography
dimer
-
2 * 21170, calculated from sequence
-
monomer
-
1 * 26349, calculated from amino acid analysis; 1 * 26500, SDS-PAGE
monomer
-
-
monomer
-
1 * 21700, muscle, SDS-PAGE; 1 * 26500, SDS-PAGE
monomer
-
1 * 21500, SDS-PAGE; 1 * 21700, calculated from amino acid analysis
monomer
-
1 * 23000, isozyme AKalpha, SDS-PAGE; 1 * 23400, isozyme AKalpha, sedimentation equilibrium in 6 M guanidine hydrochloride
monomer
-
1 * 27500, SDS-PAGE
monomer
1 * 22000, calculated from amino acid sequence
monomer
-
1 * 26000, SDS-PAGE
monomer
-
1 * 46300, SDS-PAGE; 1 * 47800, SDS-PAGE after treatment with 5 M urea
monomer
-
1 * 29500, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 32800, SDS-PAGE
monomer
-
1 * 32100, SDS-PAGE
monomer
Rhodopseudomonas rubrum
-
1 * 30900, SDS-PAGE
monomer
-
1 * 23559, calculated from nucleotide sequence
monomer
-
1 * 27000-27500, SDS-PAGE
monomer
-
-
monomer
-
1 * 24135, calculated from nucleotide sequence
monomer
-
1 * 24100, calculated from nucleotide sequence; 1 * 27000-27500, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 22000, SDS-PAGE
monomer
-
1 * 22500, cytosolic enzyme, SDS-PAGE; 1 * 28000, mitochondrial enzyme, SDS-PAGE
monomer
-
1 * 24000, muscle, SDS-PAGE; 1 * 30000, liver, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE and deduced from gene sequence
monomer
-
1 * 28000, SDS-PAGE
monomer
1 * 25000, SDS-PAGE
monomer
-
and dimer, 1 * 27000, SDS-PAGE
monomer
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry
monomer
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated
monomer
1 * 33000, recombinant adenylate kinase 2
monomer
-
iron- or zinc-bound enzyme, X-ray crystallography
monomer
-
1 * 22300, isoform ADK1, calculated from amino acid sequence; 1 * 27200, isoform ADK2, calculated from amino acid sequence
monomer
Bacillus subtilis 168
-
1 * 24100, calculated from nucleotide sequence; 1 * 27000-27500, SDS-PAGE
-
trimer
-
isozyme III, at concentrations above 3 mg/ml, dimers and trimers of MW 46000 and 68000 are formed
trimer
-
2 * 13000 + 1 * 11000, SDS-PAGE
trimer
3 * 21000, SDS-Page and deduced from gene sequence
trimer
-
crystal structure
trimer
x-ray crystallography
trimer
-
3 * 21000, SDS-Page and deduced from gene sequence
-
monomer
Thermotoga neapolitana 5068
-
1 * 25000, SDS-PAGE
-
additional information
-
two isoforms which are two conformational sub-ensembles
additional information
-
structural model of enzyme
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
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
additional information
enzyme has three catalytic domains
additional information
-
cytosolic isoform AK1 immunoprecipitates with the Kir6.2 subunit of K/ATP channel
additional information
-
expression of each of the catalytic domains. SDS-PAGE reveals 22 kDa for catalytic domain 1, 21 kDa for catalyticdomain 2 and 22 kDa for catalytic domain 3
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
-
investigation of the oligomerization behaviour of the recombinant enzyme. The preferred native form of the adenylate kinase is a homotrimer, whose existence is detected by a specific MALDI-MS strategy, correlating with the published results on adenylate oligomerization using X-ray structure analysis
additional information
-
investigation of the oligomerization behaviour of the recombinant enzyme. The preferred native form of the adenylate kinase is a homotrimer, whose existence is detected by a specific MALDI-MS strategy, correlating with the published results on adenylate oligomerization using X-ray structure analysis
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
at its N-terminus adenylate kinase 2 carries a predicted myristoylation sequence, this sequence is only present in adenylate kinase 2 of Plasmodium falciparum causing the severe tropical malaria and not in other malarial parasites, the modification significantly enhances the stability of the kinase
phosphoprotein
n vitro phosphorylation results in 19% increase of vmax
phosphoprotein
-
enzyme has three cAMP-dependent protein kinase phosphorylation sites, and can be phosphorylated in vitro. The enzymatic kinetics after phosphorylation are not significantly altered
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
muscle and liver
-
two crystal forms
-
space group P4122 or P4322
-
adenylate kinase bound to Zn2+, Co2+ or Fe2+, hanging drop vapor diffusion method, using 0.2 M sodium/potassium tartrate, 0.1 M 2-(N-morpholino)ethanesulfonic acid (pH 6.5), and 20% (w/v) PEG 200 or PEG 800
-
native enzyme in complex with Zn2+, recombinant enzymes in complex with Fe2+ or Co2+, hanging drop vapor diffusion method, using 0.2 M sodium/potassium tartrate, 0.1 M MES pH 6.5 and 20% (w/v) PEG 8K
-
analysis of atomically detailed conformational transition pathway of adenylate kinase in the absence and presence of an inhibitor. In the ligand-free state, there is no significant barrier separating the open and closed conformations. The enzyme samples near closed conformations, even in the absence of its substrate. The ligand binding event occurs late, toward the closed state, and transforms the free energy landscape. In the ligand-bound state, the closed conformation is energetically most favored with a large barrier to opening
-
atomistic molecular dynamics simulation of the complete conformational transition. Starting from the closed conformation, half-opening of the AMP-binding domain precedes a partially correlated opening of the LID and AMP-binding domain, defining the second phase. A highly stable salt bridge D118-K136 at the LID-CORE interface, contributing substantially to the total nonbonded LID-CORE interactions, is a major factor that stabilizes the open conformation
-
characterization of both ATP and AMP conformations, conformations of ATP, AMP, and the ATP analogue adenylyl imidodiphosphate
-
coarse grained model for the interplay between protein structure, folding and function. High strain energy is correlated with localized unfolding during the functional transition. Competing native interactions from the open and closed form can account for the large conformational transitions. Local unfolding may be due, in part, to competing intra-protein interactions
-
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
-
dynamics sampling simulations of the domain conformations of unliganded adenylate kinase. There is a bias towards the open-domain conformation for both domain pairs but no appreciable barrier. The interaction with the substrate enables the enzyme to adopt the closed-domain conformation. For the ATP-core domain pair, this interaction comes from a cation-pi interaction between Arg119 and the adenine moiety of ATP. For the AMP-core domain pair it is between Thr31 and the adenine moiety of AMP
-
in complex with inhibitor P1,P5-di(adenosine-5)-pentaphosphate that simulates well the binding of substrates ATP and AMP. The alpha-phosphate of AMP is well positioned for a nucleophilic attack on the gamma-phosphate of ATP, giving a stabilized pentacoordinated transition state with nucleophile and leaving group in the apical positions of a trigonal bipyramide
-
single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10C to 50C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles
-
sitting drop vapor diffusion method, using 3% (w/v) PEG 2K with 1.8-2.3 M ammonium sulfate, pH 7.0-7.3
-
solution-state NMR approach to probe the native energy landscape of adenylate kinase in its free form, in complex with its natural substrates, and in the presence of a tight binding inhibitor. 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
-
x-ray diffraction analysis
-
in complex with ADP, dADP, and Mg2+ADP-PO43-, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 1.5 M Li2SO4, 0.2 M NaCl, 0.5 mM dithiothreitol, and 25 mM MgCl2
liver; muscle
-
mutant enzyme L171P, hanging drop vapor diffusion method, 4C under conditions of 1.22-1.28 M (NH4)2SO4 and 0.1 M Tris-HCl, pH 8.5
-
with the inhibitor P1,P5-di(adenosine-5')-pentaphosphate bound to the active site, sitting drop vapor diffusion method, using 1.5 M sodium citrate pH 6.5, 150 mM sodium chloride, 0.5% n-dodecyl-N,N-dimethylamine-N-oxide, at 10C
hanging-drop vapour-diffusion method, X-ray diffraction data to 2.70 A resolution is collected, the crystal belong to space group P4(1)2(1)2 or P4(3)2(1)2. The unit-cell parameters were a = b = 76.18, c = 238.70 , alpha = beta = gamma = 90
sitting drop vapor diffusion method, using in 3.4 M ammonium chloride, 0.1 M sodium acetate (pH 4.7), and 3% ethylene glycol (v/v), at 22C
in complex with two molecules of ADP and Mg2+. Structure reveals significant conformational changes of the LID and NMP-binding domain upon substrate binding. The ternary complex represents the enzyme at the start of ATP synthesis reaction, is consistent with nucleophilic attack of a terminal oxygen from the acceptor ADP on the beta-phosphate from the donor substrate, and hints to an associative mechanism for phosphoryl transfer
-
apo isoform ADK1, hanging drop vapor diffusion method, using 100 mM Tris-HCl (pH 8.5) and 2.4 M dibasic ammonium phosphate
-
3 interconvertible crystal forms; muscle
-
muscle
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 3
-
2 h, up to 15% loss of activity
642582
2
-
1 h, at 0C, quite stable
642559
3
-
2 h, at 25C, 75% loss of activity, stable at neutral pH-values, acidic heart enzyme
642569
4
-
2 h, stable
642577
4
-
quite stable for a short time
642581
4.5
-
unstable at
642600
4.6
-
stable overnight
642577
4.8 - 11
-
stable within
693492
5
not at all stable at values below
660952
5 - 11
-
1 h stable, 0.1-0.2 mg/ml, at 0C
642572
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 4C overnight
642589
5.6
-
t1/2: 24 h, sodium phosphate buffer
642588
6 - 8
-
10 min, at 90C, in 10 mM phosphate buffer, pH 7, 0.1 M KCl, DTT, Triton X-100, +/- EDTA, 10% loss of activity within 10 min
642567
6 - 9
-
relatively stable, unstable below pH 5.5
642588
7.4 - 9.3
80% activity
660952
8
-
at least 2 days
642572
9 - 11
-
reduced ability to become renatured upon cooling below and above these pH
661349
11.5
-
1 h, at 0C, quite stable
642559
12
-
quite stable for a short time
642581
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-12
-
maximum stability
661349
4
t1/2: 29 h
661631
13
t1/2: 24 h
661631
25
-
20 h stable, pH 6-9
642574
26.5
t1/2: 12h
661631
30
-
above, 10 min, rapid loss of activity
642577
39
-
t1/2: 11 min
642600
40
-
1 h, the enzyme maintains 77.5% residual activity compared with the enzyme stored on ice
725225
43.7 - 45.3
-
the melting temperatures of Zn2+-, Co2+-, and Fe2+-containing recombinant adenylate kinases are at 45.3, 43.7, and 45.0C, respectively
704057
45
-
t1/2: 10 min
642581
45
-
pH 10, thermal denaturation
661349
50
-
enzyme type 2: in 10 mM sodium citrate buffer, pH 6, t1/2: 5 min, enzyme type 1: t1/2: 31 min
642563
52
-
the melting temperature of the free enzyme is at 52C
702283
53
12 min, wild-type 50% residual activity, mutants G40R, G64R, R128W, D140del loss of more than 90% of initial activity. At 53C, wild-type is strongly protected by presence of MgATP, mutants are unprotected with a little protection for mutant G40R; half-life 12 min, wild-type. In presence of MgATP, wild-type protein is stringly protected. Mutants G40R, G64R, R128W and D140del are not protected and completely lose activity within 12 min
673478
55
-
24 h, stable at pH 6
642582
59
-
1 h, the enzyme maintains 47% residual activity compared with the enzyme stored on ice
725225
60
-
t1/2: 2 min
642577
60
-
5 min, inactivation, 0.5 mM dithiothreitol protects
642578
60
-
t1/2: 1 min
642581
65 - 70
-
12 h, 16% loss of activity, 24 h, 23% loss of activity, variation of ionic strength or addition of substrates does not stabilize
642582
68
-
t1/2: 30 min
725225
68
-
t1/2: 4 min
725225
68
-
t1/2: 25 min
725225
68
t1/2: 43 min
725225
68
-
inclusion of 800 mM KCl sufficiently stabilizes the enzyme at 68C to observe pressure destabilization under these conditions
726705
69
-
Tm-value, wild-type enzyme
727827
73
-
Tm-value, mutant enzyme J36V
727827
74
the melting temperature is at 74C
706664
74
-
Tm-value, mutant enzyme V160J
727827
80
-
above 24 h
678510
80
-
the enzyme exhibits long-term stability (10 h) up to 80C
724106
83
-
inactivation of the enzyme in 100 mM KCl is too rapid at 83C for an accurate assessment of the effects of pressure. In the presence of 800 mM KCl, it is clear that the imposition of 50-MPa pressure has a destabilizing influence
726705
85
-
3 h, inactivation
642582
85
-
thermal denaturation of the protein starts at approx 85C due to irreversible protein aggregation
724106
86
-
Tm-value, wild-type enzyme
727827
89
-
t1/2: 6.0 min
725225
89
-
t1/2: 1.5 min
725225
89
-
t1/2: 6.0 min
725225
89
t1/2: 17 min
725225
90
-
in 10 mM phosphate buffer, pH 7, 0.1 M KCl, 0.02% Triton X-100, 2 mM DTT, +/- EDTA, t1/2: 10 min, with more than 0.2 M KCl: 10-20% loss of activity within 10 min
642567
90
up to, very stable
642614
90
-
Tm-value
724106
93.5
melting point EDTA-treated
660952
95
-
Tm-value, transition is not complete at 100C
678510
95
-
tm-value is above 95C
727827
96
-
Tm-value, mutant enzyme V160J
727827
98
-
Tm-value, mutant enzyme J36V
727827
99
-
the melting temperature of the free enzyme is at 99C
702283
99.7
melting point holoenzyme
660952
103
-
Tm-value, wild-type enzyme
727827
additional information
-
thermostability of mutant enzymes
642583
additional information
-
high thermal stability, Tm 64.8C
642619
additional information
-
the application of 50 MPa pressure does not increase the thermostability
726705
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme from Bacillus stearothermophilus is more resistant to trypsin inactivation than that from E. coli or Bacillus subtilis
-
PMSF and 5'-AMP stabilize the bovine liver enzyme, 5'-AMP stabilizes the rabbit muscle enzyme
-
stable to repeated freeze-thaw cycles, at 5-10 mg/ml
-
NADH or MgATP2- or ATP plus AMP protect against proteolysis by pronase or trypsin and against heat denaturation
-
unstable in dilute solutions and in the absence of SH-compounds
-
remarkably stable in dilute solution in the absence of any protective agent
-
2-mercaptoethanol or various metal ions do not improve recovery during purification
-
at low dithioerythritol concentrations enzyme tends to aggregate
-
bovine serum albumin, 1 mg/ml, stabilizes dilute enzyme solutions
-
diadenosine pentaphosphate, i.e. AP5A, stabilizes during preparative electrophoresis
-
in crude haemolysates type 1 enzyme is more stable than type 2, DTT or bovine serum albumin stabilizes
-
low ionic strength inactivates
-
stable to dialysis in the presence of 4 mM dithioerythritol
-
Stable to freeze-thawing
-
Triton X-100, EDTA, dithiothreitol and electrolyte protect enzyme in dilute solution and against denaturation by heat or extreme pH-values
-
unstable in dilute solution
-
unstable in dilute solution, 0.2 mg/ml, dithioerythritol, and bovine serum albumin stabilize
-
enzyme is fully active in air
-
the application of 50 MPa pressure does not increase the thermostability. Imposition of 50-MPa pressure has a destabilizing influence
-
the application of 50 MPa pressure does not increase the thermostability
-
enzyme is fully active in air
-
the application of 50 MPa pressure does not increase the thermostability
-
enzyme is fully active in air
adenylate kinase is unstable at 37C in dilute aqueous solution with a half-life of 8 min, bovine serum albumin stabilizes in part. Enzyme is also stabilized by presence of living cells such as human umbilical vein endothelial cells
-
dilution inactivates, inert proteins stabilize
-
high stability towards heat and treatment with acids
-
inactivation by contact with glass or cellophane
-
PMSF and 5'-AMP stabilize the bovine liver enzyme, 5'-AMP stabilizes the rabbit muscle enzyme
-
repeated freeze-thawing inactivates
-
stable to repeated freeze-thaw cycles, at 5-10 mg/ml
-
more stable at high concentrations or in the presence of bovine serum albumin
dithiothreitol and 2-mercaptoethanol are not necessary as protecting agents
-
stable to dilution to 0.001-0.002 mg enzyme/ml
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen enzyme solutions or lyophilized powders, wild-type and mutant enzymes, stable for weeks
-
0C, at least 2 days
-
deep frozen, 10-13% loss of activity within 6 months
-
room temperature, at least 2 days
-
-10C, partially purified, more than 1 month
-
-20C, several weeks
-
0C, a few days stable, after which activity drops to 70%, this lower specific activity can be maintained at -20C in ammonium sulfate solution for a prolonged period
-
3C, 5-10% loss within 1 month
-
4C, in distilled water, 6 weeks
-
-20C, up to 4 months
-
4C, 0.5 mg enzyme/ml, in 100 mM Tris-HCl buffer, pH 7.4, 7 days
-
frozen, in 100 mM Tris-HCl buffer, pH 7, 60% glycerol, several months
-
4C, 30% or 70% loss of activity at pH 6 or pH 5, respectively, on standing overnight
-
4C, 5 mM sodium phosphate, pH 7, 1 mM 2-mercaptoethanol, 1 month
-
frozen, up to 6 months
-
0C, at least 7 days
-
deep frozen, several weeks
-
0C, at least 7 days
-
deep frozen, several weeks
-
0C, at least 7 days
Rhodopseudomonas rubrum
-
deep frozen, several weeks
Rhodopseudomonas rubrum
-
4C, pH 6-9, 2 weeks
-
deep frozen, pH 6-9, 20 mg enzyme/ml, 4 months, but 60% loss of activity within a few days at pH 5 and 10
-
-20C, several weeks
-
-80C, 22 mM Tris-HCl, 0.5 M NaCl, pH 7.8, a few months
-
0-4C, 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-affinity column chromatography and Superdex-75 gel filtration
-
overexpressed in E. coli
-
liver mitochondria, eye lens
-
His Bind column chromatography
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
-
Blue Sepharose column chromatography and Superdex 75 gel filtration
-
no isozymes
-
Affi-Gel Blue Gel column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration
-
ammonium sulfate fractionation and Q-Sepharose column chromatography
-
single-step purification procedure from overproducing strain GT836
-
mitochondrial enzyme
-
partial, to near homogeneity
-
2 allelozymes: AK1*1 and AK1*2; and their multiple forms
-
2 allelozymes: AK1*1 and AK1*2; separable by electrophoresis, not by isoelectric focusing
-
2 isozymes, partial
-
glutathione-Sepharose column chromatography
-
GSTrap 4B column chromatography and Superdex 75 gel filtration
muscle
-
predominant form AKalpha (major form of AK-1 isozymes)
-
Sepharose column chromatography and Superdex 75 gel filtration
-
TALON metal affinity resin column chromatography
Q-XL Sepharose column chromatography, Affi-Gel Blue resin column chromatography, and Superdex-200 gel filtration
HiTrap Q-XL Sepharose column chromatography, Affi-Gel blue resin colum chromatography, and Superdex-200 gel filtration
Ni-NTA column chromatography and Superdex 200 gel filtration
-
Protino-Ni-TED column chromatography
partial, to near homogeneity
-
liver enzyme, 4 isozymes
-
muscle and liver enzyme
-