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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P35028

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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This record set is specific for:
Sulfolobus acidocaldarius
UNIPROT: P35028
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The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
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
Saci_0573
locus name
5'-AMP-kinase
-
-
-
-
adenylic kinase
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-
-
-
adenylokinase
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-
-
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kinase, adenylate (phosphorylating)
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-
-
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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
thermodynamics and kinetics
-
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
ADP + ADP
ATP + AMP
show the reaction diagram
-
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
CTP + AMP
ADP + CDP
show the reaction diagram
-
reaction at 68% the rate of ATP
-
-
?
dATP + AMP
dADP + ADP
show the reaction diagram
-
reaction at 80% the rate of ATP
-
-
?
GTP + AMP
ADP + GDP
show the reaction diagram
-
reaction at 71% the rate of AMP
-
-
?
ITP + AMP
IDP + ADP
show the reaction diagram
-
reaction at 58% the rate of ATP
-
-
?
UTP + AMP
ADP + UDP
show the reaction diagram
-
reaction at 53% the rate of AMP
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
the adenylate kinase protein preparation contains non-covalently bound ADP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
P1,P5-diadenosine 5'-pentaphosphate
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weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Thermolysin
significant increase of specific activity (1.5-fold) after a short (60 min, 50 °C) proteolytic treatment with thermolysin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
ADP
90°C, pH is not specified in the publication
1.1
AMP
90°C, pH is not specified in the publication
1.1
ATP
90°C, pH is not specified in the publication
0.65 - 0.7
ADP
-
70°C
0.5 - 1.37
AMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
170
ATP
70°C, pH is not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
kinetics
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
AMP + ATP, 70°C
6
-
AMP + ATP, 70°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7
-
about half-maximal activity at pH 3.5 and about 70% of maximal activity at pH 7, ADP + ADP, 70°C
4 - 7.5
-
about half-maximal activity at pH 4 and about 70% of maximal activity at pH 7.5, AMP + ATP, 70°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
long term incubation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 95
-
about half-maximal activity at 70°C and about 75% of maximal activity at 95°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
x * 21000, SDS-PAGE
21110
x * 21110, calculated from sequence
21170
2 * 21170, calculated from sequence
23500
-
2 * 23500, SDS-PAGE
52000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 21170, calculated from sequence
trimer
crystal structure
dimer
-
2 * 23500, SDS-PAGE
additional information
investigation of the oligomerization behaviour of the recombinant enzyme. The preferred native form of the adenylate kinase is a homotrimer, whose existence is detected by a specific MALDI-MS strategy, correlating with the published results on adenylate oligomerization using X-ray structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 3
-
2 h, up to 15% loss of activity
642582
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
thermal denaturation of the protein starts at approx 85°C due to irreversible protein aggregation
95
Tm-value, transition is not complete at 100°C
55
-
24 h, stable at pH 6
65 - 70
-
12 h, 16% loss of activity, 24 h, 23% loss of activity, variation of ionic strength or addition of substrates does not stabilize
85
-
3 h, inactivation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
overproduced in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lacher, K.; Schfer, G.
Archaebacterial adenylate kinase from the thermoacidophile Sulfolobus acidocaldarius: purification, characterization, and partial sequence
Arch. Biochem. Biophys.
302
391-397
1993
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Backmann, J.; Schafer, G.; Wyns, L.; Bonisch, H.
Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius
J. Mol. Biol.
284
817-833
1998
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Vonrhein, C.; Bonisch, H.; Schafer, G.; Schulz, G.E.
The structure of a trimeric archaeal adenylate kinase
J. Mol. Biol.
282
167-179
1998
Sulfolobus acidocaldarius (P35028), Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Schaefer, T.; Boenisch, H.; Kardinahl, S.; Schmidt, C.; Schaefer, G.
Three extremely thermostable proteins from Sulfolobuc and a reappraisal of the 'traffic rules'
Biol. Chem.
377
505-512
1996
Sulfolobus acidocaldarius (P35028), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (P35028)
Manually annotated by BRENDA team
Kath, T.; Schmid, R.; Schaefer, G.
Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
Arch. Biochem. Biophys.
307
405-410
1993
Sulfolobus acidocaldarius (P35028), Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Strupat, K.; Sagi, D.M.; Bnisch, H.; Schfer, G.; Peter-Katalinic, J.
Oligomerization and substrate binding studies of the adenylate kinase from Sulfolobus acidocaldarius by matrix-assisted laser desorption/ionization mass spectrometry
Analyst
125
563-567
2000
Sulfolobus acidocaldarius (P35028), Sulfolobus acidocaldarius DSM 639 (P35028)
-
Manually annotated by BRENDA team
Bnisch, H.; Backmann, J.; Kath, T.; Naumann, D.; Schfer, G.
Adenylate kinase from Sulfolobus acidocaldarius: expression in Escherichia coli and characterization by Fourier transform infrared spectroscopy
Arch. Biochem. Biophys.
333
75-84
1996
Sulfolobus acidocaldarius (P35028), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (P35028)
Manually annotated by BRENDA team