Linked Life Data

17294143

Source:http://linkedlifedata.com/resource/pubmed/id/17294143

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-6-25
pubmed:abstractText
We determined the cDNA-derived amino acid sequences of two arginine kinases (AK1, AK2) from the annelid Sabellastarte indica, cloned the cDNAs into pMAL plasmid and expressed them in E. coli. The phylogenetic analyses suggested that Sabellastarte AKs have evolved from a CK-related gene, not from the usual AK gene. The recombinant Sabellastarte AK1 showed a broad specificity towards various guanidine compounds, while the Sabellastarte AK2 mainly showed stronger activity for both D- and L-arginine, a very unique substrate specificity not seen before in usual AKs. We isolated guanidino compounds from the body wall musculature of Sabellastarte, and found that the major compound is D-arginine with a concentration of 4.85 +/- 0.51 mmol/kg. From these results, we suggest strongly that in Sabellastarte, D-arginine is the major phosphagen substrate and that the AK2 with substrate specificity towards D-arginine, catalyzes the phosphorylation of D-arginine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1572-3887
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-91
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
A novel arginine kinase with substrate specificity towards D-arginine.
pubmed:affiliation
Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi, 780-8520, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't