ArticleThe protein journal2007
A novel arginine kinase with substrate specificity towards D-arginine.
Article in The protein journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 26 citations in OpenAlex.
- A comprehensive review of arginine kinase proteins: What we need to know?Biochemistry and biophysics reports · 2024Review
- Broad-complex transcription factor mediates opposing hormonal regulation of two phylogenetically distant arginine kinase genes in Tribolium castaneum.Communications biology · 2020Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Identification and characterization of a putative arginine kinase homolog from Myxococcus xanthus required for fruiting body formation and cell differentiation.Journal of bacteriology · 2012Article
- Evolution of the cytoplasmic and mitochondrial phosphagen kinases unique to annelid groups.Journal of molecular evolution · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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