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Information on EC 2.7.3.5 - lombricine kinase

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EC Tree
IUBMB Comments
Also acts on methylated lombricines such as thalassemine; the specificity varies with the source species.
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This record set is specific for:
UNIPROT: Q8T6T7
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
lombricine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidinethylphosphoserine kinase
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kinase (phosphorylating), lombricine
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kinase, lombricine (phosphorylating)
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LK
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ATP:lombricine N-phosphotransferase
Also acts on methylated lombricines such as thalassemine; the specificity varies with the source species.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-53-3
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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 + lombricine
ADP + N-phospholombricine
show the reaction diagram
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?
ATP + lombricine
ADP + phospholombricine
show the reaction diagram
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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8T6T7_URECA
366
0
40941
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40941
x * 40941, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40941, calculation from nucleotide sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
substrate-free enzyme or in complex with ADP, vapor diffusion method, using 15 mM bis-Tris, 0.2 M NaNO3, 1 mM dithiothreitol, and 20% (w/v) PEG 3350MME, pH 6.8
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography, ADP-agarose column chromatography, and Superdex 200 gel filtration
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ross Ellington, W.; Bush, J.
Cloning and expression of a lombricine kinase from an echiuroid worm: Insights into structural correlates of substrate specificity
Biochem. Biophys. Res. Commun.
291
939-944
2002
Urechis caupo (Q8T6T7), Urechis caupo
Manually annotated by BRENDA team
Bush, D.J.; Kirillova, O.; Clark, S.A.; Davulcu, O.; Fabiola, F.; Xie, Q.; Somasundaram, T.; Ellington, W.R.; Chapman, M.S.
The structure of lombricine kinase: implications for phosphagen kinase conformational changes
J. Biol. Chem.
286
9338-9350
2011
Urechis caupo (Q8T6T7), Urechis caupo
Manually annotated by BRENDA team