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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Methanococcus voltae and UniProt Accession P43411

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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This record set is specific for:
Methanococcus voltae
UNIPROT: P43411
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The taxonomic range for the selected organisms is: Methanococcus voltae
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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-
-
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adenylic kinase
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-
-
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adenylokinase
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-
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kinase, adenylate (phosphorylating)
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kinase, myo- (phosphorylating)
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myokinase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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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
Mg2+
activity is Mg2+ dependent
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
1 mM, complete inhibition of ADP-dependent ATP production
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14
substrate: ATP, pH and temperature not specified in the publication
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
enzyme shows similar activity over a pH range from 6 to 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
wild-type enzyme
45
mutant enzyme J36V
53
mutant enzyme V160J
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
25°C: about 85% of maximal activity, 60°C: about 60% of maximal activity, wilde-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KADA_METVO
192
0
21303
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
x * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 25000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
1 h, the enzyme maintains 77.5% residual activity compared with the enzyme stored on ice
59
1 h, the enzyme maintains 47% residual activity compared with the enzyme stored on ice
69
Tm-value, wild-type enzyme
73
Tm-value, mutant enzyme J36V
74
Tm-value, mutant enzyme V160J
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
overexpression in Escherichia colii, 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
Criswell, A.R., Bae, E.; Stec, B.; Konisky, J.; Phillips, G.N. Jr.
Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus
J. Mol. Biol.
330
1087-1099
2003
Methanothermococcus thermolithotrophicus (P43410), Methanothermococcus thermolithotrophicus, Methanococcus voltae (P43411), Methanococcus voltae
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