Characterization of a Novel Bacterial Arginine Kinase From Desulfotalea Psychrophila

Comp Biochem Physiol B Biochem Mol Biol. 2008 Jul;150(3):312-9. doi: 10.1016/j.cbpb.2008.03.017. Epub 2008 Apr 7.


Phosphagen kinases are found throughout the animal kingdom and catalyze the transfer of a high-energy gamma phosphoryl-group from ATP to a guanidino group on a suitable acceptor molecule such as creatine or arginine. Recent genome sequencing efforts in several proteobacteria, including Desulfotalea psychrophila LSv54, Myxococcus xanthus, Sulfurovum sp. NBC37-1, and Moritella sp. PE36 have revealed what appears to be a phosphagen kinase homolog present in their genomes. Based on sequence comparisons these putative homologs bear a strong resemblance to arginine kinases found in many invertebrates and some protozoa. We describe here a biochemical characterization of one of these homologs from D. psychrophila expressed in E. coli that confirms its ability to reversibly catalyze phosphoryl transfer from ATP to arginine. A phylogenetic analysis suggests that these bacteria homologs are not widely distributed in proteobacteria species. They appear more related to protozoan arginine kinases than to similar proteins seen in some Gram-positive bacteria that share key catalytic residues but encode protein tyrosine kinases. This raises the possibility of horizontal gene transfer as a likely origin of the bacterial arginine kinases.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine Kinase / classification
  • Arginine Kinase / genetics
  • Arginine Kinase / metabolism*
  • Bacterial Proteins / classification
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Deltaproteobacteria / enzymology*
  • Eukaryota / enzymology
  • Kinetics
  • Molecular Sequence Data
  • Phylogeny
  • RNA, Transfer / metabolism
  • Sequence Alignment


  • Bacterial Proteins
  • RNA, Transfer
  • Arginine Kinase