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Information on EC 2.7.4.3 - adenylate kinase

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EC Tree
IUBMB Comments
Inorganic triphosphate can also act as donor.
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This record set is specific for:
UNIPROT: Q8TZY2
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Word Map
The enzyme appears in 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
structural maintenance of chromosome protein
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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
2 ADP
ATP + AMP
show the reaction diagram
pfSMCnbd possesses reverse adenylate kinase activity. In adenylate kinase reactions, ATP binds to its canonical binding site while AMP binds to the Q-loop glutamine and a hydration water of the Mg2+ ion. Furthermore, mutational analysis indicates that adenylate kinase reaction occurs in the engaged pfSMCnbd dimer and requires the Signature motif for phosphate transfer
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SMC_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
1177
0
135014
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the nucleotide-binding domain of the Pyrococcus furiosus structural maintenance of chromosome protein (pfSMCnbd) in complex with the adenylate kinase inhibitor P1,P5-di(adenosine-5')pentaphosphate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lammens, A.; Hopfner, K.
Structural basis for adenylate kinase activity in ABC ATPases
J. Mol. Biol.
401
265-273
2010
Pyrococcus furiosus (Q8TZY2), Pyrococcus furiosus
Manually annotated by BRENDA team