HOME
login
history
all enzymes
BRENDA home
History
Information on EC 2.7.4.3 - adenylate kinase
for references in articles please use BRENDA:EC2.7.4.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.4.3 adenylate kinaseIUBMB Comments
Inorganic triphosphate can also act as donor.
Specify your search results
Word Map
- 2.7.4.3
- phosphoenolpyruvate
- adp
- creatine
- hpr
- fructose
- nucleoside
-
permease
- streptococcus
-
phosphoenolpyruvate-dependent
- mannose
-
catabolite
- lactose
- deaminase
- 6-phosphate
- hexokinase
- autophosphorylation
- glucose-6-phosphate
- phosphoglucomutase
- mutans
- aminoglycoside
-
camp-dependent
- mannitol
- kanamycin
-
phosphofructokinase
- 2-deoxyglucose
-
intermembrane
-
antiterminator
- 5'-nucleotidase
- neomycin
- mgatp
- 6-phosphogluconate
- melibiose
-
diadenosine
-
coarse-grained
-
diphosphohydrolase
- dikinase
- phosphocreatine
-
phosphorelay
-
gamma-32patp
-
p-loop
-
bacteriocins
-
gamma-phosphate
- ganciclovir
-
transphosphorylation
- salivarius
-
2,6-bisphosphate
- phosvitin
- mucolipidosis
-
2.7.3.2
-
nptii
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
5'-AMP-kinase, ABC adenylate kinase, AD-004 like protein, adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase, adenylate kinase, adenylate kinase 1, adenylate kinase 2, adenylate kinase 4, adenylate kinase 5, adenylate kinase 6, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-AMP-kinase
-
-
-
-
adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase
-
-
adenylate kinase 1
adenylate kinase 2
adenylate kinase 4
adenylate kinase 5
isozyme, human AK5 has two separate functional domains both having enzymatic activity
adenylic kinase
-
-
-
-
adenylokinase
-
-
-
-
ADK
ADK1
AK1
AK2
AK4
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
AK6
AKlse4
AKmeso
ATP:AMP phosphotransferase
CFTR
cystic fibrosis transmembrane conductance regulator
kinase, adenylate (phosphorylating)
-
-
-
-
kinase, myo- (phosphorylating)
-
-
-
-
MJ0458
myokinase
-
-
-
-
nonstructural protein 4B
-
possesses both adenylate kinase activity and nucleotide hydrolase activity
Saci_0573
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
triphosphate can also act as donor
-
-
-
ATP + AMP = 2 ADP
mechanism
-
ATP + AMP = 2 ADP
binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites
-
ATP + AMP = 2 ADP
coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9013-02-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,N6-ethenoadenosine 5'-triphosphate + AMP
? + ADP
-
not ATP + 1,N6-ethenoadenosine 5'monophosphate
-
-
ir
2 ADP
ATP + AMP
pfSMCnbd possesses reverse adenylate kinase activity. In adenylate kinase reactions, ATP binds to its canonical binding site while AMP binds to the Q-loop glutamine and a hydration water of the Mg2+ ion. Furthermore, mutational analysis indicates that adenylate kinase reaction occurs in the engaged pfSMCnbd dimer and requires the Signature motif for phosphate transfer
-
-
?
adenosine 5'-(3-thio)triphosphate + AMP
adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
-
muscle: reaction at 97% the rate of ATP, liver mitochondria: reaction at 70% the rate of ATP
-
-
?
ADP + diphosphate
ATP + phosphate
-
at 0.1% the rate of the natural substrates
-
-
?
ATP + 7-deazaadenosine 5'-monophosphate
ADP + 7-deazaadenosine 5'-diphosphate
-
i.e. tubercidine monophosphate
-
-
?
ATP + adenine-9-beta-D-arabinofuranoside 5'-monophosphate
ADP + adenine-9-beta-D-arabinofuranoside 5'-diphosphate
-
-
-
-
?
ATP + adenosine 5'-thiophosphate
?
-
muscle: reaction at 56% the rate of AMP, liver mitochondria: reaction at 95% the rate of AMP
-
-
?
ATP + AMP-3'-diphosphate
?
-
muscle: reaction at 57% the rate of AMP, liver mitochondria: reaction at 86% the rate of AMP
-
-
?
ATP + CDP
ADP + CTP
-
-
nucleoside triphosphate synthesis by beta-phosphoryl transfer from ADP to any bound nucleoside diphosphate
-
r
ATP + shikimic acid
ADP + ?
shikimic acid is a good substrate
-
-
?
dATP + dAMP
dADP + dADP
AMP and dAMP are the preferred substrates
-
-
?
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
ADP + ADP
ATP + AMP
-
no substrates: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
-
-
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + TDP
AMP + TTP
-
Escherichia coli adenylate kinase is able to synthesize TTP, but the activity is too low to explain the high rate of TTP accumulation uring amino acid starvation of cells
-
-
?
ADP + TDP
AMP + TTP
-
rate of TTP synthesis is more than 1000000fold lower than ATP synthesis
-
-
?
AMP + H2O
ADP + phosphate
GMP can not be substituted for the AMP substrate
-
-
r
AMP + H2O
ADP + phosphate
GMP can not be substituted for the AMP substrate
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
ADP
AMP and dAMP are the preferred substrates, ATP is the best phosphate donor
-
-
?
ATP + AMP
ADP + ADP
-
ATP is the preferred phosphate donor and AMP is the best phosphate acceptor
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrates are O1-AMP, epsilon-AMP, 8-bromo-AMP, 2',3'-dialdehyde-AMP
-
r
ATP + AMP
ADP + ADP
-
in addition to the hydrolysis of NTP and NDP substrates, adenylate kinase activity is detected in purified preparations of nonstructural protein 4B with the reverse reaction ADP + ADP -> ATP + AMP, yielding a larger kcat compared to that of the forward reaction ATP + AMP -> ADP + ADP
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrates are adenosine triphosphate 3'-diphosphate, adenosine-5'-(3-thio)triphosphate/adenosine 5'-thiophosphate
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
r
ATP + AMP
ADP + ADP
-
adenylate kinase 4 shows slightly lower efficiency for the phosphorylation of AMP with ATP compared to the phosphorylation of AMP with GTP
-
-
?
ATP + AMP
ADP + ADP
adenylate kinase 5 domain AK5p1, at the assay conditions used, and at lower concentrations of substrate, AK5p1 shows generally a higher affinity for AMP compared to dAMP
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
no substrate of the reverse reaction: UDP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: adenosine tetraphosphate
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
substrates in decreasing order of activity, in the presence of Mn2+: ATP, 2'-dATP, CTP, GTP, UTP, ITP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
the adenylate kinase-catalyzed reaction requires a nucleotide complexed with Mg2+ as one substrate and a free nucleotide as the second substrate
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
the substrate pair ATP/AMP results in maximal activity
-
-
?
ATP + AMP
ADP + ADP
-
no substrates are 3',5'-cAMP, dAMP, 2'-AMP, 3'-AMP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
other NMP substrates are very poor acceptors
-
-
?
ATP + AMP
ADP + ADP
other NMP substrates are very poor acceptors
-
-
?
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
substrates in decreasing order of activity, in the presence of Mg2+: ATP, dATP, GTP, ITP
-
r
ATP + AMP
ADP + ADP
-
no substrates are adenosine, 2',3'-AMP or 3',5'-AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
no substrates are GTP/GMP, TTP/TMP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + CMP
ADP + CDP
adenylate kinase 5 domain AK5p1, the relative efficiency of CMP is about 15% compared to AMP
-
-
?
ATP + CMP
ADP + CDP
-
phosphorylation of CMP is also detected but to a lesser extend
-
-
?
ATP + dCMP
ADP + dCDP
dCMP is a poor substrate, but preferred over IMP, UMP
-
-
?
ATP + dCMP
ADP + dCDP
adenylate kinase 5 domain AK5p1, the relative efficiency of dCMP is about 15% compared to AMP
-
-
?
dATP + AMP
dADP + ADP
AMP and dAMP are the preferred substrates, dATP is a good phosphate donor
-
-
?
GTP + AMP
GDP + ADP
-
isozyme adenylate kinase 4 shows its highest efficiency when phosphorylating AMP with GTP, when GTP is used as phosphate donor only AMP is clearly phosphorylated and the phosphorylation efficiency for dAMP, CMP and dCMP is very low
-
-
?
additional information
?
-
interaction between mitochondrial adenylate kinase and nucleoside diphosphate kinase. Adenylate kinase stimulates nucleoside diphosphate kinase activity, whereas nucleoside diphosphate kinase inhibits adenylate kinase activity. the net effect may be unchanged ADP production albeit with different rates of substrate consumption
-
-
-
additional information
?
-
-
the enzyme has broader specificity for NMPs than mammalian enzymes
-
-
-
additional information
?
-
-
adenylate kinase participates in the regulation of ADP-dependent endocytosis of high-density lipoprotein by consuming the ADP generated by the ecto-F1-ATPase
-
-
-
additional information
?
-
nucleotide-binding domains 1 and 2 cannot hydrolyze ATP
-
-
-
additional information
?
-
-
adenylate kinase activity of the Mre11/Rad50 complex, which is part of a DNA repair complex, promotes DNA-DNA associations
-
-
-
additional information
?
-
-
adenylate kinase 4 catalyzes the phosphorylation of AMP, dAMP,CMPand dCMP with ATP or GTP as phosphate donors and also phosphorylates AMP with UTP as phosphate donor
-
-
-
additional information
?
-
AK5p1 phosphorylates AMP, CMP, dAMP and dCMP with ATP or GTP as phosphate donors, AK5p2 phosphorylates AMP, CMP and dAMP when ATP is used as phosphate donor and AMP, CMP and dCMP with GTP as phosphate donor, AK5p2 cannot phosphorylate dAMP in the presence of GTP
-
-
-
additional information
?
-
CINAP has previously been designated as an adenylate kinase AK6, but is very atypical as it exhibits unusually broad substrate specificity, structural features characteristic of ATPase/GTPase proteins (Walker motifs A and B) and also intrinsic ATPase activity
-
-
-
additional information
?
-
-
the enzyme catalyzes the phosphorylation of AMP (highest affinity), dAMP, CMP and dCMP with ATP as phosphate donor, while only AMP and CMP are phosphorylated when GTP is the phosphate donor. With ATP or GTP as phosphate donor it was possible to detect the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP as enzymatic products from the corresponding diphosphate substrates
-
-
-
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides
-
-
-
additional information
?
-
nucleotide-binding domain 1 cannot hydrolyze ATP
-
-
-
additional information
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
additional information
?
-
monophosphates: IMP, GMP, CMP, UMP: activity below 1%
-
-
-
additional information
?
-
-
when replacing AMP by GMP, UMP or IMP the measured activity is less than 1%
-
-
-
additional information
?
-
when replacing AMP by GMP, UMP or IMP the measured activity is less than 1%
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
at the measured in vivo concentrations of ADP of 0.114 mM, at pH 7.6, the axonemal adenylate kinase could contribute31%, and creatine kinase 69%, of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme. The three catalytic domains of adenylate kinase are considerably divergent from each other
-
-
-
additional information
?
-
-
at the measured in vivo concentrations of ADP of 0.114 mM, at pH 7.6, the axonemal adenylate kinase could contribute31%, and creatine kinase 69%, of the total non-mitochondrial ATP synthesis associated with the demembranated axoneme. The three catalytic domains of adenylate kinase are considerably divergent from each other
-
-
-
additional information
?
-
-
ATP + IMP 0.1% activity, ATP + GMP 0.3% activity
-
-
-
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + TDP
AMP + TTP
-
Escherichia coli adenylate kinase is able to synthesize TTP, but the activity is too low to explain the high rate of TTP accumulation uring amino acid starvation of cells
-
-
?
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
?
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
-
-
-
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
facilitates storage and use of the high energy of the adenine nucleotides, involved in maintenance of equilibrium among adenine nucleotides and maintenance of energy charge, important to energy economy of living systems
-
-
r
ADP + ADP
?
-
provides unique buffering role against rapid concentration changes of any component of the adenylate pool
-
-
-
additional information
?
-
interaction between mitochondrial adenylate kinase and nucleoside diphosphate kinase. Adenylate kinase stimulates nucleoside diphosphate kinase activity, whereas nucleoside diphosphate kinase inhibits adenylate kinase activity. the net effect may be unchanged ADP production albeit with different rates of substrate consumption
-
-
-
additional information
?
-
-
adenylate kinase participates in the regulation of ADP-dependent endocytosis of high-density lipoprotein by consuming the ADP generated by the ecto-F1-ATPase
-
-
-
additional information
?
-
-
adenylate kinase activity of the Mre11/Rad50 complex, which is part of a DNA repair complex, promotes DNA-DNA associations
-
-
-
additional information
?
-
-
the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides
-
-
-
additional information
?
-
-
adenylte kinase-catalysed ADP production in the vicinity of K/ATP channels is involved in channel regulation
-
-
-
additional information
?
-
-
secretion of adenylate kinase 1 is required for extracellular ATP synthesis in myotubes
-
-
-
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
Rad50 adenylate kinase activity is required for DNA tethering
-
-
-
additional information
?
-
-
adenylate kinase activity Is required for Mre11/Rad50-mediated DNA tethering
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
the adenylate kinase protein preparation contains non-covalently bound ADP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cobalt
Fe2+
K+
Li+
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
Mg2+
Mn2+
Na+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like Na+
NH4+
Zinc
Zn2+
additional information
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
Rhodopseudomonas rubrum
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; requirement
Ca2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+; less effective than Mg2+; metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Ca2+
the enzyme is slightly activated by Ca2+ (85% relative activity at 5 mM)
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+; metal ion forms complex with di- or trinucleotide; requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+; less effective than Mg2+; metal ion forms complex with di- or trinucleotide; requirement, as good as Mg2+
Ca2+
-
binding of substrates also takes place in the absence of metal ions; in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+; requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
Co2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Cobalt
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Cobalt
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Fe2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
K+
the enzyme is highly activated by K+, the optimal concentration is 10 mM
K+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like K+
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
the enzyme activity is highly dependent on Mg2+, and the optimal concentration of Mg2+ is 2 mM
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
direct Mg2+ binding activates adenylate kinase from Escherichia coli in addition to ATP-complexed Mg2+, Mg2+ can bind to adenylate kinase directly prior to AMP binding
Mg2+
-
MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
the adenylate kinase-catalyzed reaction requires a nucleotide complexed with Mg2+ as one substrate and a free nucleotide as the second substrate, maximum enzyme activity when [Mg2+]/[ATP] equals 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+; MgADP- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
binding of substrates also takes place in the absence of metal ions; in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+; inhibits at high concentrations; requirement
Mg2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; requirement; residual activity even in the presence of EDTA
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis; forms complex with di- or trinucleotide; MgADP- is true substrate; MgATP2- is true substrate; requirement
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mn2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
forms complex with di- or trinucleotide; in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
binding of substrates also takes place in the absence of metal ions; Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
NH4+
the enzyme is highly activated by NH4+ (93.6% relative activity at 5 mM)
NH4+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like NH4+
Zinc
-
0.4 mol of cobalt and 0.3 mol of zinc per mol of protein. Presence of three sulfydryl groups of cysteines potentially bound to Co2+ or Zn2+. Bound Zn2+ or Co2+ is clearly present in the LID domain and tetrahedrally coordinated to 129Cys, 135His, 151Cys, and 154Cys. Site 129Cys-X5-His-X15-Cys-X2-Cys is responsible for chelating zinc or cobalt
Zn2+
-
0.8-1 mol Zn2+ for wild-type and mutants H138N, D153C and D153T, 0.6 mol Zn2+ for mutant D153T, or 0.34 mol Zn2+ for mutant C130H per mol protein, atomic absorption spectrophotometry
Zn2+
-
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Zn2+
-
requirement, tightly bound, 0.8 mol Zn2+ per mol protein, atomic absorption spectrophotometry
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+; in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+; residual activity even in the presence of EDTA
Zn2+
-
contains one Zn2+ per enzyme molecule. EDTA treatments of 1 h at 75°C or 80°C is necessary to deplete the enzyme from its Zn2+. Presence of four Zn2+ liganding cysteines. Zn2+ is not necessary for enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-deazaadenosine 5'-monophosphate
-
i.e. tubercidine 5'-monophosphate
adenosine 5'-(beta,gamma-imido)triphosphate tetralithium
-
non-metabolizable ATP analogue, inhibition of adenylate kinase abolishes the stimulatory effect of AMP on K/ATP channels
Ag+
-
Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
cystine
-
adenylate kinase activity is diminished in the brain cortex of rats loaded with cystine dimethylester (0.0016 mg/g body weight), co-administration with cysteamine (0.00046 mg/g body weight) prevents inhibition of adenylate kinase caused by cystine
D-glucose
-
elevated concentrations of glucose inhibit cytosolic isoform AK1 expression. Inhibition of adenylate kinase increases the ATP/ADP ratio in the microenvironment of the K/ATP channel promoting channel closure and insulin secretion
P1,P4-bis(adenosine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P4-di(uridine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P5-(bis adenosine)-5'-pentaphosphate
inhibited activity of the recombinant enzyme, also inhibited the growth of L. donovani promastigotes in vitro
-
P1,P5-(diadenosine-5')-pentaphosphate
adenylate kinase-specific inhibitor
sulfur
-
elemental sulfur, reversible by dithiothreitol, muscle, not liver isozyme
suramin
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
uridine adenosine tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: mitochondrial enzyme; only cytosolic
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses; strong for muscle enzyme, less effective with dystrophic muscle or liver enzymes
8-anilino-1-naphthalenesulfonic acid
-
i.e. ANS, isoform N1 binds rapidly, isoform N2 converts to N1 and binds thereafter
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
adenosine 5'-pentaphosphate
-
inhibits the RAD50 phosphoryl transfer reaction but not ATP hydrolysis
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
Antibodies against bovine muscle enzyme
-
raised in rabbits, inactivation of muscle type, but not liver type enzyme
-
ascorbate
-
at enzyme concentration above 200 nM, no inhibition. At concentrations below 200 nM, adenylate kinase becomes increasingly sensitive to ascorbate inhibition which is accompanied by a deviation from linear relatioship between enzyme concentration and activity to a concave relationship. Aldolase reverse inhibition by ascorbate
diadenosine polyphosphate
inhibits adenylate kinase activity of the nucleotide-binding domains 1 and 2 of CFTR
-
diadenosine polyphosphate
inhibits adenylate kinase activity of the nucleotide-binding domain 1 of CFTR
-
KCl
-
no inhibitory up to 150 mM, 65% residual activity at 700 mM
Mg2+
-
strong inhibition in catalyzed reaction is observed when Mg2+concentration is in excess
Mg2+
-
at high concentrations; required for enzyme activity at low concentrations
P1,P4-diadenosine tetraphosphate
-
i.e. P1,P4-bis(5'-adenosyl)-tetraphosphate, transition state analogue, kinetics
P1,P5-bis(adenosine-5'-)pentaphosphate
i.e. Ap5A, a two substrate-mimicking inhibitor, binding affinity of SpAdK to Ap5A is determined by isothermal titration calorimetry
P1,P5-di(adenosine-5') pentaphosphate
-
Ap5A, interacts simultaneously with an AMP-binding site and ATP-binding site 2
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to Rad50 phosphoryl transfer reaction but not to ATP hydrolysis
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
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
-
inhibition of adenylate kinase prevents the stimulatory effect of AMP on K/ATP channels
P1,P5-di(adenosine-5')pentaphosphate
-
completely abolishes adenylate kinase activity but does not affect ATPase activity
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
-
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
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-diadenosine 5'-pentaphosphate
adenylate kinase-specific inhibitor, potent inhibitor of CINAP
P1,P5-diadenosine 5'-pentaphosphate
-
competitive for formation of ADP, noncompetitive for formation of ATP
P1,P5-diadenosine 5'-pentaphosphate
-
i.e. AP5A or P1,P5-bis(5'-adenosyl)-pentaphosphate, bisubstrate analogue; kinetics
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
-
not inhibitory: P1,P2-di(adenosine-5')diphosphate, P1,P3-di(adenosine-5') triphosphate, triphosphate, tetrahexaphosphate, tetrametaphosphate, hexametaphosphate
-
additional information
not inhibitory: atractyloside, chloroquine, primaquine, artemisinine, mefloquine
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
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 inhibitory: p-chloromercuribenzoate
-
additional information
-
effect of varios intermediary metabolites; no inhibition by K+, Na+, NH4+, AsO2, citrate, NADH, fructose 6-phosphate, 2-phosphoglyceraldehyde
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
induction of cellular ATP production via adenylate kinase resulting in regulation of ADP-dependent endocytosis of high-density lipoprotein
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
Thermolysin
-
significant increase of specific activity (1.5-fold) after a short (60 min, 50 °C) proteolytic treatment with thermolysin
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3 - 1.37
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
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
0.247
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, 16°C; pH 7.6, 16°C, enzyme from sperm flagellum; pH 7.6, isolated flagella
2.2
ADP
in 100 mM Tris–HCl (pH 7.5), 20 mM glucose, 5 mM MgCl2, 10 mM KCl, 2 mM dithiothreitol, at 37°C