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1,N6-ethenoadenosine 5'-triphosphate + AMP
? + ADP
-
not ATP + 1,N6-ethenoadenosine 5'monophosphate
-
-
ir
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
-
-
?
AMP + H2O
ADP + phosphate
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 + CDP
ADP + AMP + CTP
-
-
-
-
r
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 + H2O
ADP + phosphate
ATP + IMP
ADP + IDP
IMP is a poor substrate
-
-
?
ATP + shikimic acid
ADP + ?
shikimic acid is a good substrate
-
-
?
ATP + TMP
ADP + TDP
TMP is a good substrate
-
-
?
dATP + dAMP
dADP
-
-
-
-
r
dATP + dAMP
dADP + dADP
AMP and dAMP are the preferred substrates
-
-
?
dCTP + AMP
dCDP + ADP
-
-
-
-
?
dTTP + AMP
dTDP + ADP
-
-
-
-
?
GTP + AMP + CDP
GDP + AMP + CTP
-
-
-
-
?
TTP + AMP
TDP + ADP
-
-
-
-
?
additional information
?
-
2 ADP
ATP + AMP
-
-
-
r
2 ADP
ATP + AMP
-
-
-
-
?
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
2 ADP
ATP + AMP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
-
-
r
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
2 ADP
ATP + AMP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
-
-
r
2 ADP
ATP + AMP
-
-
-
-
?
2 ADP
ATP + AMP
the Escherichia coli-produced recombinant enzyme preferrs forward reaction that produces ATP
-
-
r
2 ADP
ATP + AMP
the Escherichia coli-produced recombinant enzyme prefers forward reaction that produces ATP
-
-
r
2 ADP
ATP + AMP
-
-
-
-
?
2 ADP
ATP + AMP
XP_019937160.1
-
-
-
r
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
-
-
?
2 ADP
ATP + AMP
-
-
-
-
?
ADP
AMP + ATP
-
-
-
-
r
ADP
AMP + ATP
Megalodesulfovibrio gigas
-
-
-
-
r
ADP
ATP + AMP
-
-
-
-
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 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
?
-
involved in energy metabolism
-
-
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
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
no substrates: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
-
-
?
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
no substrates: IDP, GDP
-
-
r
ADP + ADP
ATP + AMP
-
no substrate: UDP
-
-
r
ADP + ADP
ATP + AMP
-
no substrates: adenosine tetraphosphate
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
Rhodopseudomonas rubrum
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
no substrate: CDP
-
-
r
ADP + ADP
ATP + AMP
-
no substrates: IDP, GDP
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
-
-
-
r
ADP + ADP
ATP + AMP
-
no substrates: IDP, GDP
-
-
r
ADP + ADP
ATP + AMP
-
no substrate: UDP
-
-
r
ADP + ADP
ATP + AMP
-
no substrate: dADP
-
-
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 + ATP
ADP
-
-
-
?
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
-
-
-
?
ATP + AMP
2 ADP
AMP and dAMP are the preferred substrates, ATP is the best phosphate donor
-
-
?
ATP + AMP
2 ADP
-
ATP and AMP are the preferred substrates
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
the enzyme is involved in regulating concentration of ATP in cells
-
-
?
ATP + AMP
2 ADP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
ATP + AMP
2 ADP
electrostatic interactions determine entrance and release order of substrates in the catalytic cycle of adenylate kinase
-
-
?
ATP + AMP
2 ADP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
-
-
r
ATP + AMP
2 ADP
the enzyme has 3 domains, the LID, NMP, and CORE domains, that undergo large conformational rearrangements during catalytic cycle of adenylate kinase. The pathway from open to closed forms is explored using coarse-grained molecular dynamics trajectories of adenosine kinase calculated by GROMACS using a SMOG model and classify the conformations within the resultant trajectories by K-means clustering
-
-
?
ATP + AMP
2 ADP
the results of the study are more consistent with proposals that adenylate kinase belongs to a group of enzymes in which substrate binding is the predominant mechanism for driving the protein into a catalytically active state, rather than the population-shift model
-
-
?
ATP + AMP
2 ADP
the results of the study are more consistent with proposals that adenylate kinase belongs to a group of enzymes in which substrate binding is the predominant mechanism for driving the protein into a catalytically active state, rather than the population-shift model
-
-
?
ATP + AMP
2 ADP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
ATP + AMP
2 ADP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
-
-
r
ATP + AMP
2 ADP
the enzyme has 3 domains, the LID, NMP, and CORE domains, that undergo large conformational rearrangements during catalytic cycle of adenylate kinase. The pathway from open to closed forms is explored using coarse-grained molecular dynamics trajectories of adenosine kinase calculated by GROMACS using a SMOG model and classify the conformations within the resultant trajectories by K-means clustering
-
-
?
ATP + AMP
2 ADP
the enzyme is involved in regulating concentration of ATP in cells
-
-
?
ATP + AMP
2 ADP
electrostatic interactions determine entrance and release order of substrates in the catalytic cycle of adenylate kinase
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
tracking of the catalytic cycle of adenylate kinase by ultraviolet photodissociation mass spectrometry
-
-
?
ATP + AMP
2 ADP
Megalodesulfovibrio gigas
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
XP_019937160.1
the molar ratio for ATP:ADP:AMP in the equilibrium state of the reaction is about 1:1:1
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
ATP is the preferred phosphate donor and AMP is the best phosphate acceptor
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
best substrates
-
r
ATP + AMP
ADP + ADP
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
-
less specific for ATP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
-
-
r
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
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
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
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
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
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
best substrates
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are dGTP/AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are dGTP/AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
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 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
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/GMP
-
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
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
Megalodesulfovibrio gigas
-
-
-
?
ATP + AMP
ADP + ADP
Megalodesulfovibrio gigas
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
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
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
-
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
-
no substrates are ATP/UMP
-
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
-
no substrates are ITP/ADP, ATP/UDP
-
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
-
other NMP substrates are very poor acceptors
-
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
Q7Z0H0
-
-
-
?
ATP + AMP
ADP + ADP
Q14EL6
the substrate pair ATP/AMP results in maximal activity
-
-
?
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
highly specific
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/dGMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are 3',5'-cAMP, dAMP, 2'-AMP, 3'-AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/TMP
-
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 ATP/GMP
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
Rhodopseudomonas rubrum
-
-
-
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
-
best substrates
-
?
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
?
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
?
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 ATP/GMP
-
?
ATP + AMP
ADP + ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
-
?
ATP + AMP
ADP + ADP
-
no substrates are adenosine, 2',3'-AMP or 3',5'-AMP
-
r
ATP + AMP
ADP + ADP
-
no substrate of the reverse reaction: CDP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
specific for ATP, AMP and ADP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are GTP/GMP, TTP/TMP
-
r
ATP + AMP
ADP + ADP
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/TMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
best substrates
-
r
ATP + AMP
ADP + ADP
-
highly specific for AMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are GMP, UMP, CMP
-
r
ATP + AMP
ADP + ADP
-
less specific for ATP
-
r
ATP + AMP
ADP + ADP
-
specificity for AMP-site is much more rigorous than for ATP-site
-
r
ATP + AMP
ADP + ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
?
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
-
-
-
?
ATP + AMP
ADP + ADP
-
adenylate kinase isoform G
-
-
?
ATP + AMP
ADP + ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/GMP
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
no substrate of the reverse reaction: UDP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/IMP
-
r
ATP + AMP
ADP + ADP
-
no substrate of the reverse reaction: dADP
-
r
ATP + AMP
ADP + ADP
-
no substrates of the reverse reaction: IDP, GDP
-
r
ATP + AMP
ADP + ADP
-
no substrate: ATP alone
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/UMP
-
r
ATP + AMP
ADP + ADP
-
no substrates are ATP/GMP
-
r
ATP + CMP
ADP + ?
-
reaction at 1% the rate of AMP
-
-
?
ATP + CMP
ADP + ?
-
-
-
?
ATP + CMP
ADP + ?
-
reaction at 10% the rate of AMP
-
-
?
ATP + CMP
ADP + CDP
CMP is a good substrate
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
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 + CMP
ADP + CDP
-
adenylate kinase isoform G
-
-
?
ATP + dAMP
ADP + dADP
-
reaction at 30% the rate of AMP
-
-
?
ATP + dAMP
ADP + dADP
-
-
-
-
?
ATP + dAMP
ADP + dADP
-
2'-dAMP or 3'-dAMP
-
-
?
ATP + dAMP
ADP + dADP
-
reaction at 10% the rate of AMP
-
-
?
ATP + dAMP
ADP + dADP
adenylate kinase 5 domain AK5p1
-
-
?
ATP + dAMP
ADP + dADP
dAMP is the poorest substrate
-
-
?
ATP + dAMP
ADP + dADP
-
-
-
-
r
ATP + dAMP
ADP + dADP
-
reaction at 11% the rate of AMP
-
?
ATP + dAMP
ADP + dADP
-
reaction at 46% the rate of AMP
-
-
?
ATP + dAMP
ADP + dADP
-
reaction at 7% the rate of AMP
-
-
?
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
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
r
ATP + H2O
ADP + phosphate
-
-
-
r
ATP + UMP
ADP + UDP
UMP is a poor substrate
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
adenylate kinase isoform G
-
-
?
CDP + CDP
CTP + CMP
-
-
-
?
CDP + CDP
CTP + CMP
-
poor substrate
-
-
?
CTP + AMP
ADP + CDP
-
reaction at 12% the rate of ATP
-
-
?
CTP + AMP
ADP + CDP
-
-
-
-
?
CTP + AMP
ADP + CDP
-
reaction at about 3% the rate of ATP
-
-
?
CTP + AMP
ADP + CDP
-
reaction at 13% the rate of ATP
-
?
CTP + AMP
ADP + CDP
-
reaction at 68% the rate of ATP
-
-
?
CTP + AMP
ADP + CDP
-
-
-
-
?
CTP + AMP
ADP + CDP
-
reaction at 13% the rate of ATP
-
-
?
CTP + AMP
CDP + ADP
-
-
-
-
?
CTP + AMP
CDP + ADP
-
-
-
-
?
CTP + AMP
CDP + ADP
Q7Z0H0
-
-
-
?
CTP + AMP
CDP + ADP
Q14EL6
15% activity compared to ATP
-
-
?
CTP + AMP
CDP + ADP
-
adenylate kinase isoform G
-
-
?
dATP + AMP
dADP + ADP
-
-
-
-
?
dATP + AMP
dADP + ADP
-
at the same rate as ATP
-
-
?
dATP + AMP
dADP + ADP
AMP and dAMP are the preferred substrates, dATP is a good phosphate donor
-
-
?
dATP + AMP
dADP + ADP
-
-
-
-
?
dATP + AMP
dADP + ADP
-
-
-
-
?
dATP + AMP
dADP + ADP
-
reaction at about 50% the rate of ATP
-
-
?
dATP + AMP
dADP + ADP
-
-
-
-
?
dATP + AMP
dADP + ADP
-
-
-
-
?
dATP + AMP
dADP + ADP
-
at the same rate as ATP
-
-
?
dATP + AMP
dADP + ADP
-
reaction at 80% the rate of ATP
-
-
?
dATP + AMP
dADP + ADP
-
reaction at about 50% the rate of ATP
-
-
?
dATP + AMP
dADP + ADP
-
reaction at 25% the rate of ATP
-
-
?
dGTP + AMP
dGDP + ADP
-
-
-
-
?
dGTP + AMP
dGDP + ADP
-
-
-
-
?
GTP + AMP
ADP + GDP
-
reaction at 5% the rate of AMP
-
-
?
GTP + AMP
ADP + GDP
-
-
-
-
?
GTP + AMP
ADP + GDP
-
reaction at 13% the rate of AMP
-
?
GTP + AMP
ADP + GDP
-
reaction at 71% the rate of AMP
-
-
?
GTP + AMP
ADP + GDP
-
-
-
-
?
GTP + AMP
ADP + GDP
-
reaction at 3% the rate of AMP
-
-
?
GTP + AMP
GDP + ADP
-
-
-
-
?
GTP + AMP
GDP + ADP
-
-
-
-
r
GTP + AMP
GDP + ADP
-
-
-
-
?
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
-
-
?
GTP + AMP
GDP + ADP
Q7Z0H0
-
-
-
?
GTP + AMP
GDP + ADP
Q14EL6
8.4% activity compared to ATP
-
-
?
GTP + AMP
GDP + ADP
-
adenylate kinase isoform G
-
-
?
ITP + AMP
IDP + ADP
-
-
-
-
?
ITP + AMP
IDP + ADP
-
reaction at 10% the rate of ATP
-
-
?
ITP + AMP
IDP + ADP
-
not ATP/IMP
-
-
?
ITP + AMP
IDP + ADP
Q7Z0H0
-
-
-
?
ITP + AMP
IDP + ADP
Q14EL6
7.2% activity compared to ATP
-
-
?
ITP + AMP
IDP + ADP
-
poor substrate
-
-
?
ITP + AMP
IDP + ADP
-
9% the rate of ATP
-
-
?
ITP + AMP
IDP + ADP
-
not ATP/IMP
-
-
?
ITP + AMP
IDP + ADP
-
reaction at 58% the rate of ATP
-
-
?
ITP + AMP
IDP + ADP
-
adenylate kinase isoform G
-
-
?
ITP + AMP
IDP + ADP
-
8% the rate of ATP
-
-
?
UTP + AMP
ADP + UDP
-
reaction at 20% the rate of AMP
-
-
?
UTP + AMP
ADP + UDP
-
-
-
-
?
UTP + AMP
ADP + UDP
-
reaction at 11% the rate of AMP
-
?
UTP + AMP
ADP + UDP
-
reaction at 53% the rate of AMP
-
-
?
UTP + AMP
ADP + UDP
-
-
-
-
?
UTP + AMP
ADP + UDP
-
reaction at 12% the rate of AMP
-
-
?
UTP + AMP
UDP + ADP
-
-
-
-
?
UTP + AMP
UDP + ADP
-
-
-
-
?
UTP + AMP
UDP + ADP
Q7Z0H0
-
-
-
?
UTP + AMP
UDP + ADP
Q14EL6
1.4% activity compared to ATP
-
-
?
UTP + AMP
UDP + ADP
-
adenylate kinase isoform G
-
-
?
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
?
-
-
overview: substrate specificity
-
-
?
additional information
?
-
-
overview: substrate specificity
-
-
?
additional information
?
-
-
overview: substrate specificity
-
-
?
additional information
?
-
-
the enzyme has broader specificity for NMPs than mammalian enzymes
-
-
?
additional information
?
-
-
overview: substrate specificity
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
overview: substrate specificity
-
-
?
additional information
?
-
-
adenylate kinase is involved in the control of the rate of glycolysis
-
-
?
additional information
?
-
Q7Z0H0
monophosphates: IMP, GMP, CMP, UMP: activity below 1%
-
-
?
additional information
?
-
-
monophosphates: IMP, GMP, CMP, UMP: activity below 1%
-
-
?
additional information
?
-
Q14EL6
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
?
-
-
no substrate: AMP, adenosine
-
-
?
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.
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
-
-
?
additional information
?
-
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
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 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
?
-
involved in energy metabolism
-
-
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
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
the enzyme is involved in regulating concentration of ATP in cells
-
-
?
ATP + AMP
2 ADP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
ATP + AMP
2 ADP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
-
r
ATP + AMP
2 ADP
the enzyme is involved in regulating concentration of ATP in cells
-
-
?
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
2 ADP
-
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
r
ATP + AMP
ADP + ADP
-
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Li+
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
Na+
-
30 nM of AK loses about 75% of its activity but regains activity losses owing to the presence of monovalent salts like Na+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
can replace Mg2+, Ca2+ or Mn2+ less efficiently, slight activation
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
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+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ba2+
-
forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
less effective than Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Ca2+
-
in decreasing order of efficiency, but not for reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
the enzyme is slightly activated by Ca2+ (85% relative activity at 5 mM)
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
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+, Co2+, Mn2+, Zn2+
Ca2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Ca2+
-
less effective than Mg2+
Ca2+
-
binding of substrates also takes place in the absence of metal ions
Ca2+
-
in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Ca2+
-
requirement, as good as Mg2+
Ca2+
-
in decreasing order of efficiency: Mg2+, Ca2+ Mn2+, Ba2+
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Ca2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Ca2+
-
residual activity even in the presence of EDTA
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Ca2+
-
metal ion forms complex with di- or trinucleotide
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
Megalodesulfovibrio gigas
-
-
Co2+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Co2+
Co2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
about 50% as effective as Mg2+
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
can replace Mg2+, Mn2+ or Ca2+ less efficiently
Co2+
-
about 50% as effective as Mg2+
Cobalt
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Cobalt
Megalodesulfovibrio gigas
-
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+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Fe2+
Fe2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
Fe2+
Rhodopseudomonas rubrum
-
slight activation
K+
the enzyme is highly activated by K+, the optimal concentration is 10 mM
K+
150 mM, optimal concentration
K+
maximum stimulation at 100 mM
K+
maximum stimulation at 100 mM
K+
maximum stimulation at 400 mM
K+
maximum stimulation at 200 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+
K+
XP_019937160.1
100 mM, optimal concentration
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
in decreasing order of efficiency, but no reaction of ADP + ADP: Mg2+, Co2+, Ca2+, Mn2+, Ni2+
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
-
MgADP- is true substrate
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
the enzyme activity is highly dependent on Mg2+, and the optimal concentration of Mg2+ is 2 mM
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
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+
-
MgATP2- is true substrate
Mg2+
-
MgADP- is true substrate
Mg2+
-
MgATP2- is true substrate
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
Megalodesulfovibrio gigas
required for activity
Mg2+
activity is Mg2+ dependent
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mg2+
-
MgATP2- is true substrate
Mg2+
-
maximal activity when MgCl2/ADP-ratio: about 0.5 and MgCl2/ATP-ratio: 1
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
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+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
-
MgADP- is true substrate
Mg2+
Rhodopseudomonas rubrum
-
requirement
Mg2+
Rhodopseudomonas rubrum
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mg2+
Rhodopseudomonas rubrum
-
MgADP- is true substrate
Mg2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mg2+
-
MgATP2- is true substrate
Mg2+
-
binding of substrates also takes place in the absence of metal ions
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
in decreasing order of efficiency: Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mg2+
-
MgADP- is true substrate
Mg2+
-
inhibits at high concentrations
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
no absolute requirement: 20% of activity in its absence
Mg2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Mg2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Mg2+
-
residual activity even in the presence of EDTA
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
required for activity
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgATP2- is true substrate
Mg2+
-
enzymatic reaction resembles inorganic metal catalysis
Mg2+
-
MgADP- is true substrate
Mg2+
-
forms complex with di- or trinucleotide
Mg2+
-
MgADP- is true substrate
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency: Mg2+, Mn2+, Ca2+, Co2+
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+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
requirement, about 50% as effective as Mg2+
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
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+
-
in decreasing order of efficiency: Mg2+, Ca2+, Mn2+, Ba2+
Mn2+
-
binding of substrates also takes place in the absence of metal ions
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
Mg2+ and Ca2+, equally efficient, Co2+, Mn2+, Ni2+
Mn2+
-
requirement, about 25% as effective as Mg2+
Mn2+
-
in decreasing order of efficiency, substrates ADP + ADP: Mg2+, Mn2+, Zn2+, Ca2+
Mn2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Mn2+
-
residual activity even in the presence of EDTA
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
forms complex with di- or trinucleotide
Mn2+
-
requirement, about 50% as effective as Mg2+
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
-
0.3 mol of cobalt and 0.1 mol of zinc per mol of protein
Zinc
Megalodesulfovibrio gigas
-
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+
-
in decreasing order of efficiency: Mg2+, Ca2+, Co2+, Mn2+, Zn2+
Zn2+
-
1 mol per mol of enzyme, residual activity after loss
Zn2+
-
requirement, tightly bound, 0.8 mol Zn2+ per mol protein, atomic absorption spectrophotometry
Zn2+
Megalodesulfovibrio gigas
-
-
Zn2+
Megalodesulfovibrio gigas
the native enzyme contains 0.03 mol zinc per mole of protein
Zn2+
Megalodesulfovibrio gigas
the recombinant enzyme can contain Zn2+
Zn2+
Megalodesulfovibrio gigas
adenylate kinase contains a bivalent metal ion (zinc, cobalt, or iron)
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+
Zn2+
-
in decreasing order of efficiency, substrates AMP + ATP: Mg2+, Mn2+, Ca2+, Zn2+
Zn2+
-
residual activity even in the presence of EDTA
Zn2+
1 mol/mol recombinant enzyme
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
additional information
the enzyme is not activated by Mn2+
additional information
-
the enzyme is not activated by Mn2+
additional information
-
no activation by Sr2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
(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)
7-deazaadenosine 5'-monophosphate
-
i.e. tubercidine 5'-monophosphate
8-anilino-1-naphthalenesulfonic acid
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
adenosine 5'-tetraphosphate
-
weak
adenosine-5'-pentaphosphate
-
weak
Ag+
-
Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
Antibodies against bovine muscle enzyme
-
arginine phosphate
-
weak
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
diadenosine polyphosphate
-
diphosphate
-
reverse reaction
Methylmercury nitrate
-
-
p-chloromercuriphenylsulfonate
-
-
p-Hydroxymercuribenzene sulfonic acid
-
-
P1,P4-bis(adenosine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P4-di(adenosine) tetraphosphate
-
P1,P4-di(adenosine-5') tetraphosphate
-
Ap4A
P1,P4-di(uridine-5')tetraphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
P1,P4-diadenosine tetraphosphate
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
Q14EL6
adenylate kinase-specific inhibitor
P1,P5-bis(adenosine-5'-)pentaphosphate
P1,P5-di(adenosine-5') pentaphosphate
P1,P5-di(adenosine-5')pentaphosphate
P1,P5-diadenosine 5'-pentaphosphate
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
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: liver enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
not: mitochondrial enzyme; only cytosolic
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
muscle enzyme
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)
-
not: liver enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses; not: mitochondrial enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
not
5,5'-dithiobis(2-nitrobenzoic acid)
-
DTT reverses
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
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
ADP
-
in excess, substrate inhibition
ADP
-
in excess, substrate inhibition
ADP
Rhodopseudomonas rubrum
-
in excess, substrate inhibition
Ag2+
-
-
Ag2+
-
predomoninantly muscle type isozymes
Ag2+
-
predomoninantly muscle type isozymes
AMP
-
substrate inhibition
AMP
-
substrate inhibition
AMP
1 mM, complete inhibition of ADP-dependent ATP production
AMP
Rhodopseudomonas rubrum
-
product inhibition
AMP
above 0.007 mM, strong
AMP
-
above 1 mM; substrate inhibition
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
Ca2+
51% inhibition at 1 mM
Ca2+
-
51% inhibition at 1 mM
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
-
EDTA
-
and other complexing agents
F-
-
not
F-
Rhodopseudomonas rubrum
-
-
Hg2+
-
-
Hg2+
-
strong, not reaction of ADP + ADP
homologous antibodies
-
-
-
homologous antibodies
-
-
-
homologous antibodies
-
-
-
homologous antibodies
-
-
-
homologous antibodies
-
-
-
IAA
-
not
IAA
-
temperature-dependent
iodoacetate
-
not
iodoacetate
-
temperature-dependent
iodoacetate
Rhodopseudomonas rubrum
-
not
KCl
-
no inhibitory up to 150 mM, 65% residual activity at 700 mM
KCl
Megalodesulfovibrio gigas
-
not inhibitory up to 150 mM, 65% residual activity at 700 mM
Mg2+
-
at a high Mg:ATP ratio
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
N-ethylmaleimide
-
-
NADH
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
strong, reversible by GSH or cysteine
P1,P4-diadenosine tetraphosphate
-
i.e. P1,P4-bis(5'-adenosyl)-tetraphosphate, transition state analogue, kinetics
P1,P4-diadenosine tetraphosphate
-
weak
P1,P4-diadenosine tetraphosphate
-
-
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-bis(adenosine-5'-)pentaphosphate
i.e. Ap5A
P1,P5-di(adenosine-5') pentaphosphate
-
-
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
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
1 µM
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
-
-
P1,P5-di(adenosine-5')pentaphosphate
-
inhibitory to both serum adenylate kinase and endothelial adenylate kinase
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-di(adenosine-5')pentaphosphate
-
-
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
Q7Z0H0
-
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 inhibitor 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
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
strong
P1,P5-diadenosine 5'-pentaphosphate
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
adenylate kinase-specific inhibitor, potent inhibitor of CINAP
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
-
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
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
Rhodopseudomonas rubrum
-
kinetics
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
weak
P1,P5-diadenosine 5'-pentaphosphate
-
-
P1,P5-diadenosine 5'-pentaphosphate
-
specific inhibitor
P1,P5-diadenosine 5'-pentaphosphate
-
i.e. AP5A or P1,P5-bis(5'-adenosyl)-pentaphosphate, bisubstrate analogue; kinetics
phosphoenolpyruvate
-
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
additional information
-
not inhibitory: citrate
-
additional information
not inhibited by N-ethylmaleimide
-
additional information
-
not inhibited by N-ethylmaleimide
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
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: p-chloromercuribenzoate
-
additional information
-
not inhibitory: P1,P2-di(adenosine-5')diphosphate, P1,P3-di(adenosine-5') triphosphate, triphosphate, tetrahexaphosphate, tetrametaphosphate, hexametaphosphate
-
additional information
Q7Z0H0
not inhibitory: atractyloside, chloroquine, primaquine, artemisinine, mefloquine
-
additional information
-
not inhibitory: atractyloside, chloroquine, primaquine, artemisinine, mefloquine
-
additional information
-
not inhibitory: p-chloromercuribenzoate
-
additional information
-
-
-
additional information
-
not inhibitory: citrate
-
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
Rhodopseudomonas rubrum
-
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
-
additional information
not inhibitory: EDTA 10mM
-
additional information
-
not inhibitory: EDTA 10mM
-
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0.85
2'-dAMP
-
cosubstrate ATP, pH 7.4, 27°C
0.73
7-deazaadenosine 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
1.3 - 1.37
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
additional information
additional information
-
0.006
2 ADP
-
cosubstrate ADP, pH 7.8, 25°C
-
0.006
2 ADP
-
ADP in form of MgADP-
-
0.088
2 ADP
-
ADP in form of MgADP-
-
0.15
2 ADP
-
cosubstrate AMP
-
0.15
2 ADP
-
ADP in form of MgADP-
-
0.15
2 ADP
-
ADP in form of MgADP-
-
0.003
ADP
-
cosubstrate MgADP-, pH 7.8, 25°C
0.046
ADP
-
25°C, pH 8.1, isoform N2
0.11
ADP
-
cosubstrate ATP, pH 8.5
0.128
ADP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.165
ADP
Megalodesulfovibrio gigas
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, 16°C, recombinant enzyme
0.24 - 0.27
ADP
Rhodopseudomonas rubrum
-
-
0.24 - 0.27
ADP
-
25°C, pH 7.6
0.247
ADP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.28
ADP
nucleotide-binding domain 2 of wild type
0.3
ADP
nucleotide-binding domain 1 of wild type
0.32
ADP
pH 7.6, 16°C, enzyme from sperm flagellum
0.32
ADP
pH 7.6, isolated flagella
0.32
ADP
-
enzyme from sperm flagella, pH 7.6, 16°C
0.34 - 0.35
ADP
-
25°C, pH 8.0
0.34 - 0.35
ADP
-
cosubstrate ATP
0.34 - 0.35
ADP
-
pH 8.7, 25°C
0.45 - 0.55
ADP
-
30°C, pH 7.4
0.69
ADP
pH 7.6, 16°C, enzyme from embryonic cilia
0.69
ADP
-
enzyme from cilia, pH 7.6, 16°C
1.3
ADP
90°C, 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 37°C
0.03
ADP3-
-
pH 8, 25°C
0.09 - 0.092
ADP3-
-
pH 7.5, 30°C
0.09 - 0.092
ADP3-
-
25°C, pH 8.0
0.09 - 0.092
ADP3-
-
pH 8.7, 25°C
0.09 - 0.092
ADP3-
-
ATP production
0.09 - 0.092
ADP3-
-
ATP production
0.09 - 0.092
ADP3-
-
ADP, 30°C
0.0014
AMP
recombinant adenylate kinase 4, using GTP as cosubstrate
0.0053
AMP
recombinant adenylate kinase 4, using ATP as cosubstrate
0.00959
AMP
at 30°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.011
AMP
wild-type, pH 7.2, 27°C
0.013
AMP
mutant Q199R, pH 7.2, 27°C
0.016
AMP
wild-type, pH 7.2, 35°C
0.0214
AMP
at 22°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.0216
AMP
at 40°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.024
AMP
mutant Q199R, pH 7.2, 35°C
0.024
AMP
at 30°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.026
AMP
wild-type, pH 7.2, 45°C
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 40°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.038 - 0.04
AMP
-
cosubstrate ATP, 30°C
0.038 - 0.04
AMP
-
pH 7.4, 27°C
0.038 - 0.04
AMP
-
pH 7.5, 25°C, ADP production
0.04
AMP
nucleotide-binding domain 2 of wild type
0.04
AMP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.046
AMP
mutant Q199R, pH 7.2, 45°C
0.046
AMP
Megalodesulfovibrio gigas
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, 55°C
0.048
AMP
-
in 50 mM Tris-HCl pH 7.6, 5 mM MgCl2, at 37°C
0.05
AMP
Q7Z0H0
pH 6.0 and pH 7.4
0.05547
AMP
at 60°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.06
AMP
nucleotide-binding domain 1 of wild type
0.069
AMP
-
cosubstrate MgATP, pH 7.8, 25°C
0.07
AMP
mutant G40R, 37°C, pH 8.0
0.07
AMP
mutant G40R, 37°C
0.07
AMP
wild-type, pH 7.2, 60°C
0.071
AMP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.07389
AMP
at 50°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.076 - 0.083
AMP
-
25°C, pH 8.0
0.08
AMP
mutant G64R, 37°C, pH 8.0
0.08
AMP
mutant G64R, 37°C
0.081
AMP
-
25°C, pH 8.1, isoform N1
0.094
AMP
mutant Q199R, pH 7.2, 55°C
0.11
AMP
mutant Q199R, pH 7.2, 60°C
0.114 - 0.13
AMP
-
pH 8.5
0.172
AMP
adenylate kinase 5 domain AK5p1, with ATP as phosphate donor
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
Q14EL6
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C
0.38
AMP
wild-type, 37°C, pH 8.0
0.5 - 0.6
AMP
-
cosubstrate ATP, 70°C
0.547
AMP
-
25°C, pH 8.1, isoform N2
1.01
AMP
mutant Y164C, 37°C, pH 8.0
1.01
AMP
mutant Y164C, 37°C
1.039
AMP
-
25°C, pH 8.1, isoform N1
1.1
AMP
90°C, pH is not specified in the publication
1.6
AMP
mutant R11128W, 37°C, pH 8.0
1.6
AMP
mutant R128W, 37°C
1.7
AMP
mutant D140del, 37°C, pH 8.0
1.7
AMP
mutant D140del, 37°C
0.000063
ATP
-
isoenzyme AK1, membrane protein fraction
0.000141
ATP
-
isoenzyme AK1b, cytosolic protein fraction
0.00073
ATP
-
isoenzyme AK1b, membrane protein fraction
0.000998
ATP
-
isoenzyme AK1, cytosolic protein fraction
0.0018
ATP
at 30°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 6 5mM KCl
0.002
ATP
at 22°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.002
ATP
at 40°C, in 25 mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl
0.00537
ATP
at 30°C, 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 40°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.025
ATP
-
cosubstrate AMP, pH 7.8, 25°C
0.025
ATP
-
ATP in form of MgATP2-
0.034
ATP
Megalodesulfovibrio gigas
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, 37°C
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, 27°C
0.048 - 0.051
ATP
-
cosubstrate AMP, 30°C
0.049
ATP
Megalodesulfovibrio gigas
Co2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.06
ATP
mutant G40R, 37°C, pH 8.0
0.06
ATP
mutant G40R, 37°C
0.06
ATP
-
ATP in form of MgATP2-
0.07
ATP
nucleotide-binding domain 2 of wild type
0.072
ATP
-
25°C, pH 8.1, isoform N2
0.072
ATP
-
ATP in form of MgATP2-
0.075
ATP
Q14EL6
recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C
0.076
ATP
Megalodesulfovibrio gigas
Fe2+-containing recombinant adenylate kinase, in 50 mM Tris-HCl, pH 7.6, 100 mM KCl, 0.25 mM MgCl2
0.08
ATP
nucleotide-binding domain 1 of wild type
0.084
ATP
-
cosubstrate 2'-dAMP, 27°C, 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 50°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.13
ATP
-
25°C, pH 8.1, isoform N1
0.13
ATP
wild-type, 37°C, pH 8.0
0.13
ATP
-
ATP in form of MgATP2-
0.1349
ATP
at 60°C, in 25 mM phosphate buffer (pH 7.2), 5 mM MgCl2
0.23
ATP
-
ATP in form of MgATP2-
0.27 - 0.3
ATP
-
25°C, pH 8.0
0.27 - 0.3
ATP
-
cosubstrate 3'-dAMP, pH 7.4, 27°C
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, 37°C, pH 8.0
0.38
ATP
mutant G64R, 37°C
0.4
ATP
mutant D140del, 37°C, pH 8.0
0.4
ATP
mutant D140del, 37°C
0.5
ATP
mutant Y164C, 37°C, pH 8.0
0.5
ATP
mutant Y164C, 37°C
1.03
ATP
mutant R11128W, 37°C, pH 8.0
1.03
ATP
mutant R128W, 37°C
1.1
ATP
90°C, pH is not specified in the publication
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
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
-
kinetic constants of adenylate kinases from various sources
-
additional information
additional information
single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10°C to 50°C. 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
-
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metabolism
-
adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
malfunction
-
adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness
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 knockdown in larvae by RNA interference causes larval growth defects, including body weight decrease and development delay. Adenylate kinase 2 knockdown in larvae also decreases the number of circulating hemocytes
malfunction
-
depletion of adenylate kinase 2 (AK2) by RNAi impairs adiponectin secretion in 3T3-L1 adipocytes, immunoglobulin M secretion in BCL1 cells, and the induction of the unfolded protein response during differentiation of both cell types. Depletion of AK2 results in changes in adipocyte energy homeostasis, but these effects do not detectably impair key adipocyte properties such as mitochondrial biogenesis and triglyceride storage
malfunction
-
the absence of denylate kinase 6 reduces stem elongation but does not delay development
malfunction
rrecombinant expression of wild-type adk gene in fucose-inducible strains rescues a growth defect, but expression of the Arg89 mutant does not. Lack of functional SpAdK causes a growth defect in vivo, SpAdK deficiency abolishes pneumococcal growth
malfunction
adenylate kinase deficiency disrupts cell energetics and causes severe human diseases. Knockdown of overexpressed AK2 in human lung adenocarcinoma cells suppresses proliferation, migration, and invasion as well as induced apoptosis and autophagy
physiological function
adenylate kinase 4 is a unique member of the adenylate kinases family which shows no enzymatic activity in vitro
physiological function
maternally provided adenylate kianse 2 is sufficient for embryonic development, adenylate kinase 2 plays a critical role in adenine nucleotide metabolism in the mitochondrial intermembrane space and is essential for growth in Drosophila melanogaster
physiological function
-
adenylate kinase 2 regulates cell growth, viability, and proliferation in insect growth and development
physiological function
-
adenylate kinase 6 is an essential stem growth factor in Arabidopsis
physiological function
-
nuclear adenylate kinase isoform is involved in ribosome biogenesis by performing ribosomal 18S RNA processing by direct interaction with ribosomal protein TcRps14
physiological function
adenylate kinases play a critical role in intercellular homeostasis by the interconversion of ATP and AMP to two ADP molecules
physiological function
SpAdK plays an essential role in pneumococcal growth and ATP synthesis, the enzyme is essential for growth through its catalytic activity, it controls cell growth via cellular energy homeostasis. SpAdK increases total cellular ATP levels regulated by fucose in the fucose-inducible strain
physiological function
adenylate kinase is an antigen that induces high cellular and antibody responses in active TB patients
physiological function
adenylate kinase is the critical enzyme in the metabolic monitoring of cellular adenine nucleotide homeostasis. It also directs adenylate kinase/AMP/adenine nucleotide translocase signaling controlling cell cycle and proliferation, and ATP energy transfer from mitochondria to distribute energy among cellular processes. Adenylate kinase 2 and mitochondrial creatine kinase interplay in malignant transformation. Adenylate kinase modulate tumor cell response to survive under oxidative stress
physiological function
adenylate kinase potentiates the capsular polysaccharide by modulating Cps2D in Streptococcus pneumoniae D39. Interaction between SpAdK and Cps2D plays an important role in enhancing Cps2D phosphorylation, which results in increased synthesis of capsular polysaccharide
physiological function
-
cytosolic adenylate kinase is required for yeast viability. The relative fitness of the yeast strains is depending on the level of adenylate kinase activity
physiological function
-
during seed imbibition, adenylate balance is rapidly restored from the AMP stock by the concerted action of adenylate kinase and mitochondria
physiological function
MeADK2 might play a vital role in energy homeostasis in cassava mitochondria
physiological function
XP_019937160.1
the enzyme catalyzes a principal step in adenine nucleotide metabolism and cellular energy homeostasis
physiological function
the enzyme catalyzes a principal step in adenine nucleotide metabolism and cellular energy homeostasis
physiological function
the enzyme is involved in regulating concentration of ATP in cells
physiological function
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
physiological function
the enzyme plays an important role in cellular energy homeostasis
physiological function
the human vitreous fluid is responsible for maintaining an inflammatory status in diabetic eyes
physiological function
the reaction is a major player in cellular energy homeostasis and the isoform network of adenylate kinase plays an important role in AMP metabolic signaling circuits
physiological function
-
cytosolic adenylate kinase is required for yeast viability. The relative fitness of the yeast strains is depending on the level of adenylate kinase activity
-
physiological function
-
adenylate kinase is an antigen that induces high cellular and antibody responses in active TB patients
-
physiological function
-
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
-
physiological function
-
the reaction is a major player in cellular energy homeostasis and the isoform network of adenylate kinase plays an important role in AMP metabolic signaling circuits
-
physiological function
-
the enzyme is involved in regulating concentration of ATP in cells
-
additional information
Arg89 is a key active site residue, enzyme structure comparisons
additional information
-
Arg89 is a key active site residue, enzyme structure comparisons
additional information
-
ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. The active center of an adenylate kinase comprises separate ATP- and AMP-binding sites, and comprises ATP-binding site 2. Construction of a three-dimensional model of the CFTR NBD1-NBD2 heterodimer, molecular modelling with bound ATP molecules, overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ANK, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1DVR, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ZIN, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
-
enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 2BBW, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
the ligand-free enzyme structure reveals an open conformation
additional information
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
additional information
-
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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11000
-
2 * 13000 + 1 * 11000, SDS-PAGE
13000
-
2 * 13000 + 1 * 11000, SDS-PAGE
21110
x * 21110, calculated from sequence
21170
2 * 21170, calculated from sequence
21200
-
muscle, sedimentation equilibrium
21635
x * 22000, SDS-PAGE, x * 21635, calculated
22300
-
1 * 22300, isoform ADK1, calculated from amino acid sequence
22940
-
sedimentation equilibrium
23400
-
1 * 23400, isozyme AKalpha, sedimentation equilibrium in 6 M guanidine hydrochloride
23559
-
1 * 23559, calculated from nucleotide sequence
23560
-
calculated from nucleotide sequence
24100
-
calculated from nucleotide sequence
24135
-
1 * 24135, calculated from nucleotide sequence
24140
-
calculated from nucleotide sequence
24500
Megalodesulfovibrio gigas
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated
24800
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry
25200
-
liver, sedimentation equilibrium
25400
-
sedimentation equilibrium
25500
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry
26349
-
1 * 26349, calculated from amino acid analysis
26350
-
calculated from amino acid analysis
26500
-
1 * 26500, SDS-PAGE
26700
x * 26700, His12-tagged enzyme ADK1, estimated from SDS-PAGE
26900
-
acidic isozyme, PAGE
27200
-
1 * 27200, isoform ADK2, calculated from amino acid sequence
27600
Q7Z0H0
calculated without His-tag
29500
-
1 * 29500, SDS-PAGE
30900
Rhodopseudomonas rubrum
-
1 * 30900, SDS-PAGE
31000
-
liver, gel filtration
32000
-
1 * 32000, SDS-PAGE
32500
Q14EL6
estimated from amino acid sequence
32800
-
1 * 32800, SDS-PAGE
34000
Q14EL6
estimated from SDS-PAGE
40000
-
sucrose density gradient centrifugation
46300
-
1 * 46300, SDS-PAGE
47800
-
1 * 47800, SDS-PAGE after treatment with 5 M urea
48500
-
x * 48500, calculated from amino acid sequence
50000
-
and 25000, gel filtration and non-reducing SDS-PAGE
53000
SDS-PAGE, fused with the GST tag the recombinant protein has a size of about 53000 Da
63000
gel filtration, sedimentation analysis
130000
-
x * 130000, SDS-PAGE
130000
x * 130000, full-length enzyme, 21000, recombinant expression of catalytic domain 1 or 3, 22000, recombinant expression of catalytic domain 2, SDS-PAGE
21000
-
muscle, sedimentation and diffusion
21000
-
electrospray ionization mass spectroscopy
21000
x * 21000, SDS-PAGE
21000
3 * 21000, SDS-Page and deduced from gene sequence
21300
-
-
21300
-
sedimentation equilibrium
21300
-
isozyme AKalpha, sedimentation equilibrium
21500
-
-
21500
-
muscle, gel filtration
21500
-
liver mitochondria
21700
-
amino acid analysis
21700
-
1 * 21700, muscle, SDS-PAGE
22000
-
gel filtration
22000
-
sedimentation equilibrium
22000
XP_019937160.1
SDS-PAGE, gel filtration
22000
SDS-PAGE, gel filtration
22000
calculated from amino acid sequence
22000
-
adenylate kinase 1, SDS-PAGE
22000
x * 22000, SDS-PAGE
22000
-
2 * 22000 isoenzyme AK1, SDS-PAGE
22000
x * 22000, SDS-PAGE, x * 21635, calculated
22500
-
isozyme AKalpha, gel filtration
22500
-
1 * 22500, cytosolic enzyme, SDS-PAGE
22600
-
titration of 2 SH-groups
22600
-
x * 22600, calculated from amino acid sequence
23000
-
-
23000
-
muscle, gel filtration
23000
-
isozyme III, at concentrations above 3 mg/ml, dimers and trimers of MW 46000 and 68000 are formed
23000
-
1 * 23000, SDS-PAGE
23000
-
1 * 23000, isozyme AKalpha, SDS-PAGE
23000
-
2 * 23000 isoenzyme AK1b, SDS-PAGE
23500
-
gel filtration
23500
-
2 * 23500, SDS-PAGE
24000
-
24000
-
x * 24000, SDS-PAGE
24000
-
1 * 24000, muscle, SDS-PAGE
24700
Megalodesulfovibrio gigas
-
gel filtration
24700
Megalodesulfovibrio gigas
estimated from SDS-PAGE
24700
Megalodesulfovibrio gigas
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated
25000
-
SDS-PAGE
25000
-
and 50000, gel filtration and non-reducing SDS-PAGE
25000
1 * 25000, SDS-PAGE
25000
-
x * 25000, SDS-PAGE
25000
x * 25000, SDS-PAGE
25000
-
1 * 25000, SDS-PAGE and deduced from gene sequence
25000
-
x * 25000, adenylate kinase-like protein 1, SDS-PAGE
25000
x * 25000 (approximately), SDS-PAGE
25000
x * 25000 (approximately), SDS-PAGE
25000
x * 25000 (approximately), SDS-PAGE
25600
-
liver, sedimentation equilibrium
25600
-
x * 25600, SDS-PAGE
26000
-
gel filtration
26000
Megalodesulfovibrio gigas
-
gel filtration
26000
calculated from nucleotide sequence
26000
-
adenylate kinase 2, SDS-PAGE
27000
-
gel filtration
27000
-
and dimer, 1 * 27000, SDS-PAGE
27000
-
and monomer, 2 * 27000, SDS-PAGE
27000
-
x * 27000, calculated from amino acid sequence
28000
x * 28000, SDS-PAGE
28000
-
1 * 28000, SDS-PAGE
28000
-
1 * 28000, mitochondrial enzyme, SDS-PAGE
29000
-
-
29000
-
1 * 29000, SDS-PAGE
30000
-
gel filtration
30000
-
1 * 30000, liver, SDS-PAGE
32100
Rhodopseudomonas rubrum
-
gel filtration
32100
-
1 * 32100, SDS-PAGE
33000
Q14EL6
1 * 33000, recombinant adenylate kinase 2
33000
-
x * 33000, His-tagged enzyme, SDS-PAGE
46000 - 49000
-
analytical ultracentrifugation
46000 - 49000
-
isozyme II
additional information
-
amino acid composition
additional information
-
comparison of amino acid composition of different sources
additional information
-
comparison of amino acid composition of different sources
additional information
-
comparison of amino acid composition of different sources
additional information
-
comparison of amino acid composition of different sources
additional information
-
molecular weights of enzymes from different organisms
additional information
-
molecular weights of enzymes from different organisms
additional information
-
molecular weights of enzymes from different organisms
additional information
-
molecular weights of enzymes from different organisms
additional information
-
a great deal of homology and some distinct differences between liver and muscle type enzymes of different organisms
additional information
-
a great deal of homology and some distinct differences between liver and muscle type enzymes of different organisms
additional information
-
a great deal of homology and some distinct differences between liver and muscle type enzymes of different organisms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 22600, calculated from amino acid sequence
?
-
x * 27000-28000, SDS-PAGE
?
x * 21000-23000, SDS-PAGE
?
x * 26700, His12-tagged enzyme ADK1, estimated from SDS-PAGE
?
-
x * 27000, calculated from amino acid sequence
?
-
x * 33000, His-tagged enzyme, SDS-PAGE
?
x * 22000, SDS-PAGE, x * 21635, calculated
?
-
x * 48500, calculated from amino acid sequence
?
x * 25000 (approximately), SDS-PAGE
?
-
x * 25000 (approximately), SDS-PAGE
-
?
x * 25000 (approximately), SDS-PAGE
?
x * 25000 (approximately), SDS-PAGE
?
-
x * 25000, adenylate kinase-like protein 1, SDS-PAGE
?
x * 24000, detagged recombinant enzyme, SDS-PAGE, x * 23721, sequence calculation
?
x * 130000, full-length enzyme, 21000, recombinant expression of catalytic domain 1 or 3, 22000, recombinant expression of catalytic domain 2, SDS-PAGE
?
x * 21110, calculated from sequence
dimer
-
and monomer, 2 * 27000, SDS-PAGE
dimer
Megalodesulfovibrio gigas
cobalt-bound enzyme, X-ray crystallography
dimer
-
2 * 22000 isoenzyme AK1, SDS-PAGE
dimer
-
2 * 23000 isoenzyme AK1b, 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 * 21170, calculated from sequence
dimer
-
2 * 21170, calculated from sequence
-
homodimer
Western blot analysis, SDS-PAGE
homodimer
static light scattering
monomer
-
1 * 27000-27500, SDS-PAGE
monomer
-
1 * 24100, calculated from nucleotide sequence
monomer
-
1 * 27000-27500, SDS-PAGE
-
monomer
-
1 * 24100, calculated from nucleotide sequence
-
monomer
-
1 * 32800, SDS-PAGE
monomer
-
1 * 22000, SDS-PAGE
monomer
-
1 * 25500, SDS-PAGE, 1 * 24800, electrospray mass spectrometry
monomer
-
and dimer, 1 * 27000, SDS-PAGE
monomer
-
1 * 27000-27500, SDS-PAGE
monomer
-
1 * 23559, calculated from nucleotide sequence
monomer
1 * 22000, SDS-PAGE
monomer
-
1 * 28000, mitochondrial enzyme, SDS-PAGE
monomer
-
1 * 22500, cytosolic enzyme, SDS-PAGE
monomer
-
1 * 24135, calculated from nucleotide sequence
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 21500, SDS-PAGE
monomer
-
1 * 26500, SDS-PAGE
monomer
-
1 * 23400, isozyme AKalpha, sedimentation equilibrium in 6 M guanidine hydrochloride
monomer
-
1 * 26349, calculated from amino acid analysis
monomer
-
1 * 21700, calculated from amino acid analysis
monomer
-
1 * 23000, isozyme AKalpha, SDS-PAGE
monomer
-
1 * 21700, muscle, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
Megalodesulfovibrio gigas
-
1 * 24500, SDS-PAGE, 1 * 24700, electrospray mass spectrometry, 1 * 24500, calculated
monomer
Megalodesulfovibrio gigas
iron- or zinc-bound enzyme, X-ray crystallography
monomer
-
1 * 29500, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE and deduced from gene sequence
monomer
-
1 * 28000, SDS-PAGE
monomer
XP_019937160.1
1 * 22000, SDS-PAGE
monomer
Q14EL6
1 * 33000, recombinant adenylate kinase 2
monomer
-
1 * 24000, muscle, SDS-PAGE
monomer
-
1 * 30000, liver, SDS-PAGE
monomer
-
1 * 32100, SDS-PAGE
monomer
Rhodopseudomonas rubrum
-
1 * 30900, SDS-PAGE
monomer
-
1 * 27500, SDS-PAGE
monomer
1 * 22000, calculated from amino acid sequence
monomer
-
1 * 22300, isoform ADK1, calculated from amino acid sequence
monomer
-
1 * 27200, isoform ADK2, calculated from amino acid sequence
monomer
-
1 * 46300, SDS-PAGE
monomer
-
1 * 47800, SDS-PAGE after treatment with 5 M urea
monomer
1 * 25000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
-
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
trimer
x-ray crystallography
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
-
3 * 21000, SDS-Page and deduced from gene sequence
-
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
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
-
cytosolic isoform AK1 immunoprecipitates with the Kir6.2 subunit of K/ATP channel
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
-
structural model of enzyme
additional information
-
two isoforms which are two conformational sub-ensembles
additional information
-
enzyme has three catalytic domains
additional information
enzyme has three catalytic domains
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
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
-
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crystals of the mutant enzyme I26T are grown at 20°C by the hanging-drop method
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively
space group P4122 or P4322
-
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 10°C to 50°C. 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
-
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively
cocrystallized with bis(adenosine)-5'-tetraphosphate
crystal structure is established in complex with bis(adenosine)-5'-tetraphosphate and malonate ion or in complex with P1,P5-di(adenosine-5')pentaphosphate
crystallized in two conformations, in closed conformation with adenosine monophosphate and in open conformation without substrate
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
mutant enzyme L171P, hanging drop vapor diffusion method, 4°C 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 10°C
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
Megalodesulfovibrio gigas
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
Megalodesulfovibrio gigas
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 Å, 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 22°C
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
-
crystal structure of the nucleotide-binding domain of the Pyrococcus furiosus structural maintenance of chromosome protein (pfSMCnbd) in complex with the adenylate kinase inhibitor P1,P5-di(adenosine-5')pentaphosphate
apo isoform ADK1, hanging drop vapor diffusion method, using 100 mM Tris-HCl (pH 8.5) and 2.4 M dibasic ammonium phosphate
-
purified recombinant enzyme mutants AKm1 and AKm2 in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 30 mg/ml AKm1 or 18 mg/ml AKm2 in 10 mM HEPES pH 7.0, and 4 mM Ap5A, with an equal amount of a reservoir solution containing 18% w/v PEG 3350, 100 mM lithium sulfate, and 100 mM Bis-Tris, pH 5.5, for mutant AKm1 and containing 22% w/v PEG 3350, and 200 mM calcium chloride for mutant AKm2, 20°C, X-ray diffraction structure determination and analysis at 2.990 and 1.65 A resolution, respectively
small-scale batch method at 20°C
purified detagged recombinant enzyme free or in complex with inhibitor Ap5A, hanging drop vapour diffusion method, mixing of 0.0025 ml of 18 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 1 mM MgCl2, with 0.0025 ml of reservoir solution containing 2.0 M (NH4)2SO4, 0.1 M CHES, pH 9.5, 0.2 M Li2SO4, and 0.1 M CsCl2 for the ligand-free enzyme, and 0.1 M sodium acetate, 0.1 M sodium acetate, pH 4.6, 30% PEG 8000, and 50 mM NaF for the inhibitor-bound enzyme, 22°C, X-ray diffraction structure determination and analysis at 1.7 and 1.48 A resolution, respectively, molecular replacement using structures Marinibacillus marinus PDB ID 3FB4 and Burkholderia pseudomallei PDB ID 3GMT as search models
purified recombinant enzyme in ligand-free and inhibitor Ap5A-bound states, hanging drop vapour diffusion method, mixing of 0.0025 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 50-150 mM NaCl, 5 mM MgCl2, with 0.0025 ml reservoir solution containing 1.0 M sodium citrate, 0.1 M HEPES, pH 7.5 for the ligand-free crystals and 0.2 M sodium acetate, pH 7.2, 30% PEG 8000 for the inhibitor-bound crystals, 22°C, X-ray diffraction structure determination and analysis at 1.96 and 1.65 A resolution, respectively. SpAdK can crystallize promiscuously in different forms, and the open structure is flexible in conformation
3 interconvertible crystal forms
-
hanging-drop method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
I26T
Tm-value is 39.4°C compared to 46.4°C for wild-type enzyme
Q16L/Q199R
thermostabilization of full-length protein. Cells harboring the mutant fragment pair with concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217 show weak complementation of Escherichia coli mutant after fusion with polypeptides that strongly associate
Q199R
modest increase in stability, 3 degrees increase in melting temperature. At temperatures of 20°C to 45°C, 50% loss of activity, with subsequent increase at higher temperatures. rigidification of he overall structure through stabilization of a polypeptide loop containing R199 that is part of the ATP-binding site
I26T
-
Tm-value is 39.4°C compared to 46.4°C for wild-type enzyme
-
C149S
-
loss of zinc content and of enzymic activity
C152S
-
loss of zinc content and of enzymic activity
I28V/I118V/I173V
lower temperature stability than wild-type enzyme
F137W
-
mutation in domain that closes over the ATP binding site
F86W
-
mutation in AMP binding site
P87S
-
thermosensitive enzyme, about 50% of wild type activity
S129F
-
about 25% of wild type activity
S41W
-
mutation in domain that closes over the AMP binding site
Y133W
-
mutation in domain that closes over the ATP binding site
P17G
-
alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
P17V
-
alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
C40V
-
the mutation is associated with reticular dysgenesis
D140del
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 30% residual adenylate kinase activity
D165G
-
the mutation is associated with reticular dysgenesis
E9X
-
the mutation is associated with reticular dysgenesis
G40R
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 25% residual adenylate kinase activity
H79G
the mutation affects both adenylate kinase (enzymatic efficiency (kcat/Km) is reduced by 72% relative to the wild type enzyme) and ATPase catalytic efficiency and induces homodimer formation
K233X
-
the mutation is associated with reticular dysgenesis
K4G
when the amino acid residue is mutated, the protein is imported in mitochondria
K4G/R7G
when both amino acid residues are mutated simultaneously the protein remains in the cytosol
L1254A
-
mutant in cystic fibrosis transmembrane conductance regulator. Cystic fibrosis transmembrane conductance regulator shows adenylate kinase activity in the presence of ATP plus physiologic concentrations of AMP or ADP. P1,P5-di(adenosine-5') pentaphosphate increases the activity of the mutant. The mutation increases the EC50 for ATP by more than 10-fold and reduces channel activity by prolonging the closed state. P1,P5-di(adenosine-5') pentaphosphate changes the relationship between ATP concentration and current. At submaximal ATP concentrations, P1,P5-di(adenosine-5') pentaphosphate stimulates current by stabilizing the channel open state
L171P
the mutation dramatically changes the orientation of the LID domain, which can be described as a twisted and closed conformation in contrast to the open and closed conformations in other adenylate kinases
L183X
-
the mutation is associated with reticular dysgenesis
M1V
-
the mutation is associated with reticular dysgenesis
R103W
-
the mutation is associated with reticular dysgenesis
R128W
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 44% residual adenylate kinase activity
R186C
-
the mutation is associated with reticular dysgenesis
R7G
when the amino acid residue is mutated, the protein is imported in mitochondria
S1202R
-
mutation of RAD50 signature motif, 10-50% of wild-type activity in formation of ADP, formation of ATP is not affected
S231D
-
the mutation is associated with reticular dysgenesis
Y152T
-
the mutation is associated with reticular dysgenesis
Y164C
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 0% residual adenylate kinase activity
G551D
mutation affects the ability of the nucleotide-binding domain 1 of CFTR to dimerize, has an exaggerated nonlinear phase compared with the wild type
S48A
Tm-value is 36.0°C, compared to 33.8°C for the wild-type enzyme
T188K
Tm-value is 30.7°C, compared to 33.8°C for the wild-type enzyme
V118I
Tm-value is 36.6°C, compared to 33.8°C for the wild-type enzyme
V118I/V173I
Tm-value is 41.4°C, compared to 33.8°C for the wild-type enzyme
V173I
Tm-value is 36.3°C, compared to 33.8°C for the wild-type enzyme
V28I
Tm-value is 38.8°C, compared to 33.8°C for the wild-type enzyme
V28I/V118I/V173I
Tm-value is 45.1°C, compared to 33.8°C for the wild-type enzyme
S793R
-
mutation in Rad50 singature motif. Mutant shows lower levels of both ATPase and adenylate kinase activity relative to the wild-type enzyme, consistent with an overall deficiency in ATP binding
K13Q
-
catalytically dead but properly folded variant
K13Q
-
catalytically dead but properly folded variant
-
T26A
the Tm-value is 38.4°C compared to 42.7°C for wild-type enzyme
T26F
the Tm-value is 43.0°C compared to 42.7°C for wild-type enzyme
T26I
the Tm-value is 50.8°C compared to 42.7°C for wild-type enzyme
T26L
the Tm-value is 48.4°C compared to 42.7°C for wild-type enzyme
T26N
the Tm-value is 38.3°C compared to 42.7°C for wild-type enzyme
T26S
the Tm-value is 38.7°C compared to 42.7°C for wild-type enzyme
T26V
the Tm-value is 48.3°C compared to 42.7°C for wild-type enzyme
T26Y
the Tm-value is 44.1°C compared to 42.7°C for wild-type enzyme
R89A
site-directed mutagenesis, inactive active site mutant
S1205R
-
mutation of RAD50 signature motif, 5-10% of wild-type activity in formation of ADP, formation of ATP is not affected. Complete loss of spore viability in the wild-type/S1205R heterozygote
S1205R
-
mutation in Rad50 protein, mutant protein is expressed in yeast and forms a complete complex with Mre11. Mutant does not support spore viability. telomeres are as severely shortened as in a rad50 deletion strain
additional information
-
T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
-
T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
-
construction of chimera between the mesophilic Bacillus subtilis enzyme and the thermophilic Bacillus stearothermophilus enzyme by exchange of one or more of the seven protein segments. Analysis of the chimeras shows spatial separation of stability and activity control with specific contributions of dynamics to catalysis
additional information
no functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217. Weak complementation after fusion with polypeptides that strongly associate
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
-
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
-
additional information
treatment with RNAi results in the suppression of growth of the worm
additional information
-
treatment with RNAi results in the suppression of growth of the worm
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
-
in adenylate kinase knock-out mice, the stimulatory effect of AMP on K/ATP channels is much less pronounced, though not completely suppressed
additional information
-
knock out of the major isoform adenylate kinase 1 disrupts the synchrony between inorganic phosphate turnover at ATP-consuming sites and gamma-ATP exchange at ATP synthesis sites. This reduces energetic signal communication in the post-ischemic heart. Adenylate kinase 1 gene deletion blunts vascular adenylate kinase phosphotransfer, compromises the contractility-coronary flow relationship, and precipitates inadequate coronary reflow following ischemiareperfusion. Deficit in adenylate kinase activity abrogates AMP signal generation and reduces the vascular adenylate kinase/creatine kinase activity ratio essential for the response of metabolic sensors. The sarcolemma-associated splice variant adenylate kinase 1beta facilitates adenosine production. Adenosine treatment bypasseds adenylate kinase 1 deficiency and restores post-ischemic flow to wild-type levels
additional information
-
knock-down of adenylate kinase 1 results in block of synthesis of external ATP
additional information
-
modification of C25 with fluorescent probe IAEDANS, studies of conformatinal changes
additional information
-
transgenic plants containing a construct with an antisense fragment of the plastidial adenylate kinase gene. 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
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
construction of a conditional mutant using fucose inducible adk promoter, the D39 fucose-inducible adk strain
additional information
-
construction of a conditional mutant using fucose inducible adk promoter, the D39 fucose-inducible adk strain
additional information
-
recombinant expression of full-length enzyme and each of its three catalytic domains. No enzymic activity of a sole catalytic domain
additional information
recombinant expression of full-length enzyme and each of its three catalytic domains. No enzymic activity of a sole catalytic domain
additional information
-
expression of full-length protein and each of its three catalytic domains in Escherichia coli. Full-length protein displays high catalytic activity, while none of the catalytic domains alone is active.
additional information
-
functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 179 and C-terminus, amino acids 80220. Reconstituted enzyme has 17fold lower activity compared with full-length native enzyme
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-12
Megalodesulfovibrio gigas
-
maximum stability
103
Tm-value, wild-type enzyme
30
-
above, 10 min, rapid loss of activity
30.7
T-value, mutant enzyme T188K
33.8
T-value, wild-type enzyme
36
T-value, mutant enzyme S48A
36.6
T-value, mutant enzyme V118I
38.3
Tm-value, mutant enzyme T26N
38.4
Tm-value, mutant enzyme T26A
38.7
Tm-value, mutant enzyme T26S
38.8
T-value, mutant enzyme V28I
39.4
Tm-value, mutant enzyme I26T
40
1 h, the enzyme maintains 77.5% residual activity compared with the enzyme stored on ice
40.8
-
T-value, wild-type enzyme
41.4
T-value, mutant enzyme V118I/V173I
42.7
Tm-value, wild-type enzyme
43.7 - 45.3
Megalodesulfovibrio gigas
the melting temperatures of Zn2+-, Co2+-, and Fe2+-containing recombinant adenylate kinases are at 45.3, 43.7, and 45.0°C, respectively
44.1
Tm-value, mutant enzyme T26Y
46
30 min, 50% inactivation
46.4
Tm-value, wild-type enzyme
48.3
Tm-value, mutant enzyme T26V
48.4
Tm-value, mutant enzyme T26L
50
-
enzyme type 2: in 10 mM sodium citrate buffer, pH 6, t1/2: 5 min, enzyme type 1: t1/2: 31 min
50.8
Tm-value, mutant enzyme T26I
52
-
the melting temperature of the free enzyme is at 52°C
54
XP_019937160.1
30 min, 50% inactivation
55
-
24 h, stable at pH 6
55.8
T-value, wild-type enzyme, in presence of P1,P5-di(adenosine 5')-pentaphosphate
56.5
T-value, mutant enzyme I28V/I118V/I173V, in presence of P1,P5-di(adenosine 5')-pentaphosphate
59
1 h, the enzyme maintains 47% residual activity compared with the enzyme stored on ice
60.3
T-value, mutant enzyme V28I/V118I/V173I, in presence of P1,P5-di(adenosine 5')-pentaphosphate
61.8
T-value, wild-type enzyme, in presence of P1,P5-di(adenosine 5')-pentaphosphate
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
69
Tm-value, wild-type enzyme
73
Tm-value, mutant enzyme J36V
83
inactivation of the enzyme in 100 mM KCl is too rapid at 83°C 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
86
-
Tm-value, wild-type enzyme
93.5
melting point EDTA-treated
96
Tm-value, mutant enzyme V160J
98
Tm-value, mutant enzyme J36V
99
-
the melting temperature of the free enzyme is at 99°C
99.7
melting point holoenzyme
36.2
T-value, mutant enzyme I28V/I118V/I173V
36.2
T-value, mutant enzyme V173I
37
stable for 3 h
43
Tm-value, mutant enzyme T26F
43
-
T-value, wild-type enzyme
45
-
t1/2: 10 min
45
Megalodesulfovibrio gigas
-
pH 10, thermal denaturation
45
Rhodopseudomonas rubrum
-
t1/2: 10 min
45.1
T-value, wild-type enzyme
45.1
T-value, mutant enzyme V28I/V118I/V173I
53
12 min, wild-type 50% residual activity, mutants G40R, G64R, R128W, D140del loss of more than 90% of initial activity. At 53°C, wild-type is strongly protected by presence of MgATP, mutants are unprotected with a little protection for mutant G40R
53
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
60
-
t1/2: 1 min
60
Rhodopseudomonas rubrum
-
t1/2: 1 min
60
-
5 min, inactivation, 0.5 mM dithiothreitol protects
68
t1/2: 30 min
68
inclusion of 800 mM KCl sufficiently stabilizes the enzyme at 68°C to observe pressure destabilization under these conditions
74
the melting temperature is at 74°C
74
Tm-value, mutant enzyme V160J
80
above 24 h
80
the enzyme exhibits long-term stability (10 h) up to 80°C
85
-
3 h, inactivation
85
thermal denaturation of the protein starts at approx 85°C due to irreversible protein aggregation
89
t1/2: 6.0 min
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
95
-
tm-value is above 95°C
95
Tm-value, transition is not complete at 100°C
additional information
-
thermostability of mutant enzymes
additional information
the application of 50 MPa pressure does not increase the thermostability
additional information
-
the application of 50 MPa pressure does not increase the thermostability
additional information
the application of 50 MPa pressure does not increase the thermostability
additional information
the application of 50 MPa pressure does not increase the thermostability
additional information
-
high thermal stability, Tm 64.8°C
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adenylate kinase-like proteins 1 and 2 are expressed in Escherichia coli KRX cells
-
adk-gene, expressed in Escherichia coli
-
cloned and expressed in Escherichia coli
-
cloned into vector pET28b and expressed in Escherichia coli BL21DE3pLys cells
coexpression of adenylate kinase 2 and N-myristoyltransferase in the presence of myristate in Escherichia coli strain C-41
Q14EL6
cytosolic isoforms AK1 and AK5 are expressed in human islets and INS-1 cells. Elevated concentrations of glucose inhibit AK1 expression
-
expressed in Escherichia coli
expressed in Escherichia coli B834(DE3)pLysS cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta cells
expressed in in Sf9 insect cells
-
expression in Cos-1 cells
-
expression in Escherichia coli
expression in Escherichia coli and HeLa cell
-
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3). Adenylate kinase is used as a soluble tag to facilitate MEK1R4F protein expression and its application in large-scale phosphorylated ERK1/2 preparation and purification
-
expression in Escherichia coli strain M15
Q7Z0H0
expression in HeLa cell
-
expression of full-length protein and each of its three catalytic domains in Escherichia coli
-
gene adk, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli
gene adk, recombinant expression of wild-type adk gene in fucose-inducible strains rescues a growth defect, but expression of the Arg89 mutant does not. Recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli
overexpression in Escherichia coli, wild-type enzyme, mutant enzymes and chimeric enzymes
overexpression in Escherichia colii, wild-type enzyme, mutant enzymes and chimeric enzymes
overproduced in Escherichia coli
recombinant expression of full-length enzyme and each of its three catalytic domains
the cobalt- or iron-bound enzyme is expressed in Escherichia coli BL21(DE3) cells
Megalodesulfovibrio gigas
the His6-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
-
wild-type and mutant CFTR are transiently expressed in HeLa cell membranes a double vaccinia virus/T7 RNA polymerase system
-
wild-type and thermosensitive mutants
-
-
-
cloned into vector pET28b and expressed in Escherichia coli BL21DE3pLys cells
cloned into vector pET28b and expressed in Escherichia coli BL21DE3pLys cells
expressed in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
Megalodesulfovibrio gigas
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta cells
expressed in Escherichia coli Rosetta cells
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli
overexpression in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli
overexpression in Escherichia coli
-
overexpression in Escherichia coli
overexpression in Escherichia coli
overexpression in Escherichia coli
-
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