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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Escherichia coli and UniProt Accession P69441
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2.7.4.3 adenylate kinaseIUBMB Comments
Inorganic triphosphate can also act as donor.
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Word Map
- 2.7.4.3
- phosphoenolpyruvate
- adp
- creatine
- hpr
- fructose
- nucleoside
-
permease
- streptococcus
-
phosphoenolpyruvate-dependent
- mannose
- 6-phosphate
-
catabolite
- deaminase
- lactose
- mannitol
- hexokinase
- mutans
- glucose-6-phosphate
-
camp-dependent
- aminoglycoside
- autophosphorylation
- phosphoglucomutase
-
phosphofructokinase
- kanamycin
- neomycin
- 6-phosphogluconate
-
phosphorelay
- 5'-nucleotidase
-
antiterminator
- mgatp
- 2-deoxyglucose
-
intermembrane
-
transphosphorylation
-
gamma-phosphate
- melibiose
- salivarius
- ganciclovir
- phosphocreatine
- nptii
-
diadenosine
-
diphosphohydrolase
-
gamma-32patp
-
p-loop
-
2.7.3.2
- dikinase
-
coarse-grained
- analysis
- phosvitin
- medicine
-
2,6-bisphosphate
- mucolipidosis
- phosphoenzyme
- diagnostics
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphotransferase, adenylate kinase, myokinase, adenylate kinase 1, adenylate kinase 2, nonstructural protein 4b, cinap, adenylokinase, spadk, adenylate kinase isoenzyme 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-AMP-kinase
-
-
-
-
adenylic kinase
-
-
-
-
adenylokinase
-
-
-
-
kinase, adenylate (phosphorylating)
-
-
-
-
kinase, myo- (phosphorylating)
-
-
-
-
myokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9013-02-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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 + CDP
ADP + CTP
-
-
nucleoside triphosphate synthesis by beta-phosphoryl transfer from ADP to any bound nucleoside diphosphate
-
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
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
-
-
?
ADP + TDP
AMP + TTP
-
Escherichia coli adenylate kinase is able to synthesize TTP, but the activity is too low to explain the high rate of TTP accumulation uring amino acid starvation of cells
-
-
?
ADP + TDP
AMP + TTP
-
rate of TTP synthesis is more than 1000000fold lower than ATP synthesis
-
-
?
ATP + AMP
2 ADP
-
substrate ligand-binding modeling, detailed overview
-
-
r
ATP + AMP
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
additional information
?
-
-
the enzyme has broader specificity for NMPs than mammalian enzymes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3 - 1.37
adenine-9-beta-D-arabinofuranoside 5'-monophosphate
-
cosubstrate ATP, pH 7.4, 27°C
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00468 - 0.01326
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
0.000497 - 0.05417
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
0.00468
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
closed conformation, pH and temperature not specified in the publication
0.01326
(5E)-5-[(2-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
open conformation, pH and temperature not specified in the publication
0.000497
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
closed conformation, pH and temperature not specified in the publication
0.05417
(5E)-5-[(3-bromophenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
open conformation, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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 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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
remarkably stable in dilute solution in the absence of any protective agent
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Affi-Gel Blue Gel column chromatography, Q-Sepharose column chromatography, and S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
coarse grained model for the interplay between protein structure, folding and function which is applicable to allosteric or non-allosteric proteins. 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
additional information
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiraga, S.; Sugino, Y.
Utilisation of certain derivatives of alanine and arginine by yeasts
Biochim. Biophys. Acta
119
416-418
1966
Escherichia coli, Escherichia coli JE24F+
Noda, L.
Adenylate kinase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
8
279-305
1973
Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Citrus limon, Blattidae, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mus musculus, Physarum polycephalum, Rattus norvegicus, Sus scrofa, Thiobacillus denitrificans, Triticum aestivum
-
Haase, G.H.W.; Brune, M.; Reinstein, J.; Pai, E.F.; Pingoud, A.; Wittinghofer, A.
Adenylate kinases from thermosensitive Escherichia coli strains
J. Mol. Biol.
207
151-162
1989
Escherichia coli
Althoff, S.; Zambrowicz, B.; Liang, P.; Glaser, M.; Phillips, G.N.
Crystallization and preliminary X-ray analysis of Escherichia coli adenylate kinase [letter]
J. Mol. Biol.
199
665-666
1988
Escherichia coli
Saint Girons, I.; Gilles, A.M.; Margarita, D.; Michelson, S.; Monnot, M.; Fermandjian, S.; Danchin, A.; Brzu, O.
Structural and catalytic characteristics of Escherichia coli adenylate kinase
J. Biol. Chem.
262
622-629
1987
Escherichia coli
Glaser, P.; Prescecan, E.; Delepierre, M.; Surewicz, W.K.; Mantsch, H.H.; Brzu, O.; Gilles, A.M.
Zinc, a novel structural element found in the family of bacterial adenylate kinases
Biochemistry
31
3038-3043
1992
Geobacillus stearothermophilus, Escherichia coli
Bilderback, T.; Fulmer, T.; Mantulin, W.W.; Glaser, M.
Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase
Biochemistry
35
6100-6106
1996
Escherichia coli
Dzeja, P.P.; Zeleznikar, R.J.; Goldberg, N.D.
Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes
Mol. Cell. Biochem.
184
169-182
1998
Escherichia coli, Rattus norvegicus
Yan, H.; Tsai, M.D.
Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity
Adv. Enzymol. Relat. Areas Mol. Biol.
73
103-134
1999
Bacillus subtilis, Bos taurus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens
Lin, Y.; Nageswara Rao, B.D.
Structural Characterization of Adenine Nucleotides Bound to Escherichia coli Adenylate Kinase. 2. 31P and 13C Relaxation Measurements in the Presence of Cobalt(II) and Manganese(II)
Biochemistry
39
3647-3655
2000
Escherichia coli
Lin, Y.; Nageswara Rao, B.D.
Structural Characterization of Adenine Nucleotides Bound to Escherichia coli Adenylate Kinase. 1. Adenosine Conformations by Proton Two-Dimensional Transferred Nuclear Overhauser Effect Spectroscopy
Biochemistry
39
3636-3646
2000
Escherichia coli
Willemoes, M.; Kilstrup, M.
Nucleoside triphosphate synthesis catalysed by adenylate kinase is ADP dependent
Arch. Biochem. Biophys.
444
195-199
2005
Escherichia coli
Mueller, C.W.; Schulz, G.E.
Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. a model for a catalytic transition state
J. Mol. Biol.
224
159-177
1992
Escherichia coli
Snow, C.; Qi, G.; Hayward, S.
Essential dynamics sampling study of adenylate kinase: comparison to citrate synthase and implication for the hinge and shear mechanisms of domain motions
Proteins
67
325-337
2007
Escherichia coli
Gigliobianco, T.; Lakaye, B.; Makarchikov, A.F.; Wins, P.; Bettendorff, L.
Adenylate kinase-independent thiamine triphosphate accumulation under severe energy stress in Escherichia coli
BMC Microbiol.
8
16
2008
Escherichia coli
Aden, J.; Wolf-Watz, M.
NMR identification of transient complexes critical to adenylate kinase catalysis
J. Am. Chem. Soc.
129
14003-14012
2007
Escherichia coli (P69441)
Lu, Q.; Wang, J.
Single molecule conformational dynamics of adenylate kinase: energy landscape, structural correlations, and transition state ensembles
J. Am. Chem. Soc.
130
4772-4783
2008
Escherichia coli (P69441)
Whitford, P.C.; Gosavi, S.; Onuchic, J.N.
Conformational transitions in adenylate kinase. Allosteric communication reduces misligation
J. Biol. Chem.
283
2042-2048
2008
Escherichia coli (P69441)
Whitford, P.C.; Miyashita, O.; Levy, Y.; Onuchic, J.N.
Conformational transitions of adenylate kinase: switching by cracking
J. Mol. Biol.
366
1661-1671
2007
Escherichia coli (P69441)
Arora, K.; Brooks, C.L.
Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism
Proc. Natl. Acad. Sci. USA
104
18496-18501
2007
Escherichia coli (P69441)
Kubitzki, M.B.; de Groot, B.L.
The atomistic mechanism of conformational transition in adenylate kinase: a TEE-REX molecular dynamics study
Structure
16
1175-1182
2008
Escherichia coli
Krishnamurthy, H.; Munro, K.; Yan, H.; Vieille, C.
Dynamics in Thermotoga neapolitana adenylate kinase: 15N relaxation and hydrogen-deuterium exchange studies of a hyperthermophilic enzyme highly active at 30C
Biochemistry
48
2723-2739
2009
Escherichia coli, Thermotoga neapolitana
Pontiggia, F.; Zen, A.; Micheletti, C.
Small- and large-scale conformational changes of adenylate kinase: a molecular dynamics study of the subdomain motion and mechanics
Biophys. J.
95
5901-5912
2008
Escherichia coli
Chen, B.; Sysoeva, T.A.; Chowdhury, S.; Guo, L.; Nixon, B.T.
ADPase activity of recombinantly expressed thermotolerant ATPases may be caused by copurification of adenylate kinase of Escherichia coli
FEBS J.
276
807-815
2009
Escherichia coli
Tan, Y.W.; Hanson, J.A.; Yang, H.
Direct Mg2+ binding activates adenylate kinase from Escherichia coli
J. Biol. Chem.
284
3306-3313
2009
Escherichia coli
Beckstein, O.; Denning, E.J.; Perilla, J.R.; Woolf, T.B.
Zipping and unzipping of adenylate kinase: atomistic insights into the ensemble of open <--> closed transitions
J. Mol. Biol.
394
160-176
2009
Escherichia coli
Cukier, R.I.
Apo adenylate kinase encodes its holo form: a principal component and varimax analysis
J. Phys. Chem. B
113
1662-1672
2009
Escherichia coli
Schrank, T.P.; Bolen, D.W.; Hilser, V.J.
Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins
Proc. Natl. Acad. Sci. USA
106
16984-16989
2009
Escherichia coli (P69441), Escherichia coli
Adkar, B.V.; Jana, B.; Bagchi, B.
Role of water in the enzymatic catalysis: study of ATP + AMP -> 2ADP conversion by adenylate kinase
J. Phys. Chem. A
115
3691-3697
2011
Escherichia coli (P69441)
Daily, M.D.; Phillips, G.N.; Cui, Q.
Interconversion of functional motions between mesophilic and thermophilic adenylate kinases
PLoS Comput. Biol.
7
e1002103
2011
Aquifex aeolicus (O66490), Aquifex aeolicus, Escherichia coli (P69441), Escherichia coli
Armenta-Medina, D.; Perez-Rueda, E.; Segovia, L.
Identification of functional motions in the adenylate kinase (ADK) protein family by computational hybrid approaches
Proteins
79
1662-1671
2011
Escherichia coli (P69441)
Wang, Y.; Gan, L.; Wang, E.; Wang, J.
Exploring the dynamic functional landscape of adenylate kinase modulated by substrates
J. Chem. Theory Comput.
9
84-95
2013
Geobacillus stearothermophilus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Onuk, E.; Badger, J.; Wang, Y.J.; Bardhan, J.; Chishti, Y.; Akcakaya, M.; Brooks, D.H.; Erdogmus, D.; Minh, D.D.L.; Makowski, L.
Effects of catalytic action and ligand binding on conformational ensembles of adenylate kinase
Biochemistry
56
4559-4567
2017
Escherichia coli (P69441), Escherichia coli, Escherichia coli K12 (P69441)
Yang, F.; Li, H.
Expression of adenylate kinase fused MEK1R4F in Escherichia coli and its application in ERK phosphorylation
Biotechnol. Lett.
39
1553-1558
2017
Escherichia coli
Cui, D.; Ren, W.; Li, W.; Wang, W.
Molecular simulations of substrate release and coupled conformational motions in adenylate kinase
J. Theor. Comput. Chem.
15
1650004
2016
Escherichia coli (P69441), Escherichia coli K12 (P69441)
-
Ionescu, M.I.; Oniga, O.
Molecular docking evaluation of (E)-5-arylidene-2-thioxothiazolidin-4-one derivatives as selective bacterial adenylate kinase inhibitors
Molecules
23
1076
2018
Escherichia coli (P69441), Streptococcus pneumoniae (Q04ML5), Escherichia coli K12 (P69441)
Wang, Y.; Makowski, L.
Fine structure of conformational ensembles in adenylate kinase
Proteins
86
332-343
2018
Escherichia coli (P69441), Escherichia coli K12 (P69441)
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