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Synonyms
phosphotransferase, adenylate kinase, myokinase, adenylate kinase 1, adenylate kinase 2, nonstructural protein 4b, cinap, adenylokinase, spadk, adenylate kinase isoenzyme 1,
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adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase
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adenylate kinase 5
isozyme, human AK5 has two separate functional domains both having enzymatic activity
adenylate kinase isoenzyme 1
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adenylate kinase isozyme 2
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adenylate kinase-2
Q14EL6
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adenylate kinase-like protein 1
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AKLP1
AK5p1
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
AK5p2
domain of adenylate kinase 5, human AK5 has two separate functional domains both having enzymatic activity
ATP:AMP phosphotransferase
coilin interacting nuclear ATPase protein
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cystic fibrosis transmembrane conductance regulator
kinase, adenylate (phosphorylating)
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kinase, myo- (phosphorylating)
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nonstructural protein 4B
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possesses both adenylate kinase activity and nucleotide hydrolase activity
structural maintenance of chromosome protein
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adenylate kinase 1
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adenylate kinase 1
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isoform
adenylate kinase 2
isoform
adenylate kinase 2
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isoform
ADK
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ADK1
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AK1
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isoform
AK2
isoform
AK4
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AK5
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AK6
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AKlse4
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AKm
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AKmeso
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ATP:AMP phosphotransferase
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ATP:AMP phosphotransferase
Megalodesulfovibrio gigas
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ATP:AMP phosphotransferase
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ATP:AMP phosphotransferase
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CFTR
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cystic fibrosis transmembrane conductance regulator
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cystic fibrosis transmembrane conductance regulator
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MJ0458
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Rv0733
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Saci_0573
locus name
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ATP + AMP = 2 ADP
mechanism
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ATP + AMP = 2 ADP
mechanism
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ATP + AMP = 2 ADP
mechanism
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ATP + AMP = 2 ADP
mechanism
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ATP + AMP = 2 ADP
mechanism
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ATP + AMP = 2 ADP
iso-random bi-bi mechanism
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ATP + AMP = 2 ADP
overview: mechanism
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ATP + AMP = 2 ADP
overview: mechanism
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ATP + AMP = 2 ADP
overview: mechanism
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ATP + AMP = 2 ADP
overview: mechanism
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ATP + AMP = 2 ADP
overview: mechanism
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ATP + AMP = 2 ADP
thermodynamics and kinetics
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ATP + AMP = 2 ADP
triphosphate can also act as donor
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ATP + AMP = 2 ADP
associative mechanism for phosphoryl transfer
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ATP + AMP = 2 ADP
binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites
ATP + AMP = 2 ADP
coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover
ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
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ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
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ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
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ATP + AMP = 2 ADP
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis
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1,N6-ethenoadenosine 5'-triphosphate + AMP
? + ADP
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not ATP + 1,N6-ethenoadenosine 5'monophosphate
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ir
adenosine 5'-(3-thio)triphosphate + AMP
adenosine 5'-diphosphate + adenosine 5'-(3-thio)diphosphate
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muscle: reaction at 97% the rate of ATP, liver mitochondria: reaction at 70% the rate of ATP
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?
ADP + diphosphate
ATP + phosphate
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at 0.1% the rate of the natural substrates
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?
AMP + H2O
ADP + phosphate
ATP + 7-deazaadenosine 5'-monophosphate
ADP + 7-deazaadenosine 5'-diphosphate
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i.e. tubercidine monophosphate
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?
ATP + adenine-9-beta-D-arabinofuranoside 5'-monophosphate
ADP + adenine-9-beta-D-arabinofuranoside 5'-diphosphate
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?
ATP + adenosine 5'-thiophosphate
?
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muscle: reaction at 56% the rate of AMP, liver mitochondria: reaction at 95% the rate of AMP
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?
ATP + AMP + CDP
ADP + AMP + CTP
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r
ATP + AMP-3'-diphosphate
?
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muscle: reaction at 57% the rate of AMP, liver mitochondria: reaction at 86% the rate of AMP
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?
ATP + CDP
ADP + CTP
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nucleoside triphosphate synthesis by beta-phosphoryl transfer from ADP to any bound nucleoside diphosphate
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r
ATP + H2O
ADP + phosphate
ATP + IMP
ADP + IDP
IMP is a poor substrate
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?
ATP + shikimic acid
ADP + ?
shikimic acid is a good substrate
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?
ATP + TMP
ADP + TDP
TMP is a good substrate
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?
dATP + dAMP
dADP
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r
dATP + dAMP
dADP + dADP
AMP and dAMP are the preferred substrates
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?
dCTP + AMP
dCDP + ADP
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?
dTTP + AMP
dTDP + ADP
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?
GTP + AMP + CDP
GDP + AMP + CTP
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?
TTP + AMP
TDP + ADP
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?
additional information
?
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2 ADP
ATP + AMP
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r
2 ADP
ATP + AMP
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?
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
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r
2 ADP
ATP + AMP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
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r
2 ADP
ATP + AMP
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
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r
2 ADP
ATP + AMP
molecular simulations of substrate release and coupled conformational motions in adenylate kinase
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r
2 ADP
ATP + AMP
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?
2 ADP
ATP + AMP
the Escherichia coli-produced recombinant enzyme preferrs forward reaction that produces ATP
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r
2 ADP
ATP + AMP
the Escherichia coli-produced recombinant enzyme prefers forward reaction that produces ATP
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r
2 ADP
ATP + AMP
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?
2 ADP
ATP + AMP
XP_019937160.1
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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
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?
2 ADP
ATP + AMP
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?
ADP
AMP + ATP
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r
ADP
AMP + ATP
Megalodesulfovibrio gigas
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r
ADP
ATP + AMP
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
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?
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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facilitates transfer of high-energy phosphorylss and signal communication between mitochondria and actomyosin in cardiac muscle
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?
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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involved in energy metabolism
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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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
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r
ADP + ADP
?
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provides unique buffering role against rapid concentration changes of any component of the adenylate pool
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?
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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no substrates: adenosine 5'-(2-thio)diphosphate, adenosine diphosphate 3'-diphosphate
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?
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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no substrates: IDP, GDP
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r
ADP + ADP
ATP + AMP
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no substrate: UDP
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r
ADP + ADP
ATP + AMP
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no substrates: adenosine tetraphosphate
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
Rhodopseudomonas rubrum
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r
ADP + ADP
ATP + AMP
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r
ADP + ADP
ATP + AMP
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no substrate: CDP
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r
ADP + ADP
ATP + AMP
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no substrates: IDP, GDP
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r
ADP + ADP
ATP + AMP
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r
2.7.4.3 adenylate kinase
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