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Information on EC 2.7.4.3 - adenylate kinase and Organism(s) Danio rerio and UniProt Accession Q1L8L9

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IUBMB Comments
Inorganic triphosphate can also act as donor.
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This record set is specific for:
Danio rerio
UNIPROT: Q1L8L9
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
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
adenylate kinase 2
isoform
AK2
isoform
5'-AMP-kinase
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-
-
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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
-
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
ADP + ADP
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
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?
KAD2_DANRE
241
0
26616
Swiss-Prot
other Location (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I28V/I118V/I173V
lower temperature stability than wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.2
T-value, mutant enzyme I28V/I118V/I173V
45.1
T-value, wild-type enzyme
56.5
T-value, mutant enzyme I28V/I118V/I173V, in presence of P1,P5-di(adenosine 5')-pentaphosphate
61.8
T-value, wild-type enzyme, in presence of P1,P5-di(adenosine 5')-pentaphosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
P1,P5-di(adenosine 5')-pentaphosphate binding stabilizes the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pannicke, U.; Hoenig, M.; Hess, I.; Friesen, C.; Holzmann, K.; Rump, E.M.; Barth, T.F.; Rojewski, M.T.; Schulz, A.; Boehm, T.; Friedrich, W.; Schwarz, K.
Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2
Nat. Genet.
41
101-105
2009
Homo sapiens, Danio rerio (Q1L8L9), Danio rerio
Manually annotated by BRENDA team
Moon, S.; Kim, J.; Bae, E.
Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes
Sci. Rep.
7
16027
2017
Xiphophorus maculatus, Poecilia reticulata, Notothenia coriiceps (A0A2R2JFU5), Notothenia coriiceps, Danio rerio (Q68EH2), Danio rerio
Manually annotated by BRENDA team