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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57900

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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Methanocaldococcus jannaschii
UNIPROT: Q57900
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
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 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
ATP + AMP
2 ADP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
maximum stimulation at 100 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
P1,P5-di(adenosine-5')pentaphosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89
substrate: ATP, pH and temperature not specified in the publication
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 90
60°C: about 50% of amximal activity, 90°C: about 89% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
x * 25000 (approximately), SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 25000 (approximately), SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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°
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103
Tm-value, wild-type enzyme
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
96
Tm-value, mutant enzyme V160J
98
Tm-value, mutant enzyme J36V
additional information
the application of 50 MPa pressure does not increase the thermostability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is fully active in air
the application of 50 MPa pressure does not increase the thermostability. Imposition of 50-MPa pressure has a destabilizing influence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli, wild-type enzyme, mutant enzymes and chimeric enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rusnak, P.; Haney, P.; Konisky, J.
The adenylate kinases from a mesophilic and three thermophilic methanogenic members of the archaea
J. Bacteriol.
177
2977-2981
1995
Methanotorris igneus (P43408), Methanotorris igneus, Methanocaldococcus jannaschii (P43409), Methanocaldococcus jannaschii, Methanothermococcus thermolithotrophicus (P43410), Methanothermococcus thermolithotrophicus, Methanococcus voltae (P43411), Methanococcus voltae, Methanocaldococcus jannaschii DSM 2661 (P43409)
Manually annotated by BRENDA team
Wang, X.; Yuan, Y.; Teng, M.; Niu, L.; Gao, Y.
Crystallization and preliminary X-ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
69
1272-1274
2013
Methanocaldococcus jannaschii (Q57900), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57900)
Manually annotated by BRENDA team
Konisky, J.; Michels, P.C.; Clark, D.S.
Pressure stabilization is not a general property of thermophilic enzymes: the adenylate kinases of Methanococcus voltae, Methanococcus maripaludis, Methanococcus thermolithotrophicus, and Methanococcus jannaschii
Appl. Environ. Microbiol.
61
2762-2764
1995
Methanococcus maripaludis, Methanocaldococcus jannaschii (P43409), Methanothermococcus thermolithotrophicus (P43410), Methanococcus voltae (P43411)
Manually annotated by BRENDA team
Haney, P.J.; Stees, M.; Konisky, J.
Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus
J. Biol. Chem.
274
28453-28458
1999
Methanothermococcus thermolithotrophicus, Methanotorris igneus, Methanocaldococcus jannaschii (P43409), Methanococcus voltae (P43411), Methanocaldococcus jannaschii DSM 2661 (P43409)
Manually annotated by BRENDA team