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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Bacillus subtilis and UniProt Accession P16304

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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Bacillus subtilis
UNIPROT: P16304
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The taxonomic range for the selected organisms is: Bacillus subtilis
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, structural maintenance of chromosome protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-AMP-kinase
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adenylic kinase
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adenylokinase
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kinase, adenylate (phosphorylating)
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kinase, myo- (phosphorylating)
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myokinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + AMP = 2 ADP
show the reaction diagram
overview: mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:AMP phosphotransferase
Inorganic triphosphate can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-02-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ADP
ATP + AMP
show the reaction diagram
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r
AMP + ATP
ADP
show the reaction diagram
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-
-
?
ADP + ADP
?
show the reaction diagram
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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
ATP + AMP
show the reaction diagram
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-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
additional information
?
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-
overview: substrate specificity
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + ADP
?
show the reaction diagram
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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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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forms complex with di- or trinucleotide
Ca2+
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metal ion forms complex with di- or trinucleotide
Co2+
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can replace Mg2+, Mn2+ or Ca2+ less efficiently
Mn2+
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forms complex with di- or trinucleotide
Zn2+
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-Hydroxymercuribenzene sulfonic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.11
AMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.19
AMP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
350 - 400
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24100
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calculated from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39.4
Tm-value, mutant enzyme I26T
46.4
Tm-value, wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme from Bacillus stearothermophilus is more resistant to trypsin inactivation than that from E. coli or Bacillus subtilis
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen enzyme solutions or lyophilized powders, wild-type and mutant enzymes, stable for weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged mutant AKm1 and AKm2 enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
overexpressed in E. coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3)
gene adk, recombinant expression of His-tagged mutant AKm1 and AKm2 enzymes in Escherichia coli
adk-gene, expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Manually annotated by BRENDA team
Perrier, V.; Surewicz, W.K.; Glaser, P.; Martineau, L.; Craescu, C.T.; Fabian, H.; Mantsch, H.H.; Brzu, O.; Gilles, A.M.
Zinc chelation and structural stability of adenylate kinase from Bacillus subtilis
Biochemistry
33
9960-9967
1994
Bacillus subtilis, Bacillus subtilis 168
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bae, E.; Phillips, G.N.
Roles of static and dynamic domains in stability and catalysis of adenylate kinase
Proc. Natl. Acad. Sci. USA
103
2132-2137
2006
Bacillus subtilis
Manually annotated by BRENDA team
Counago, R.; Wilson, C.J.; Pena, M.I.; Wittung-Stafshede, P.; Shamoo, Y.
An adaptive mutation in adenylate kinase that increases organismal fitness is linked to stability-activity trade-offs
Protein Eng. Des. Sel.
21
19-27
2008
Bacillus subtilis (P16304)
Manually annotated by BRENDA team
Nguyen, P.Q.; Liu, S.; Thompson, J.C.; Silberg, J.J.
Thermostability promotes the cooperative function of split adenylate kinases
Protein Eng. Des. Sel.
21
303-310
2008
Thermotoga neapolitana, Bacillus subtilis (P16304)
Manually annotated by BRENDA team
Moon, S.; Bae, E.
Crystal structures of thermally stable adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis
J. Korean Soc. Appl. Biol. Chem.
57
661-665
2014
Bacillus subtilis (P16304), Geobacillus stearothermophilus (P27142), Sporosarcina globispora (P84139), Bacillus subtilis 168 (P16304)
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Manually annotated by BRENDA team
Mohamadnezhadi, H.; Beiramzadeh, A.; Shadman Lakmehsari, M.; Khalifeh, K.; Heshmati, E.
Temperature dependent dynamics in highly homologous adenylate kinases
J. Biomol. Struct. Dyn.
37
2110-2117
2019
Bacillus subtilis (P16304), Geobacillus stearothermophilus (P27142), Sporosarcina globispora (P84139), Bacillus subtilis 168 (P16304)
Manually annotated by BRENDA team
Moon, S.; Kim, J.; Koo, J.; Bae, E.
Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability
Struct. Dyn.
6
024702
2019
Bacillus subtilis (P16304), Sporosarcina globispora (P84139), Bacillus subtilis 168 (P16304)
Manually annotated by BRENDA team