Evolution of the arginine kinase gene family

Uda, Kouji; Fujimoto, Naka; Akiyama, Youhei; Mizuta, Kanae; Tanaka, Kumiko; Ellington, W. Ross; Suzuki, Tomohiko

doi:10.1016/j.cbd.2005.10.007

Cited by 93 publications

(88 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3), and found that the positions of all four introns of Siphonosoma HTK are homologous with those of molluscan AK genes [18,19]. The intron corresponding to the first intron in molluscan AK genes appears to have been lost in the Siphonosoma HTK gene, but the splice junctions of the remaining four introns are exactly conserved between AK and HTK genes (Fig.…”

Section: Exon/intron Organization Of Siphonosoma Htk Gene Ismentioning

confidence: 94%

Hypotaurocyamine kinase evolved from a gene for arginine kinase

2005

Self Cite

View full text Add to dashboard Cite

Hypotaurocyamine kinase (HTK) is a member of the highly conserved family of phosphagen kinases that includes creatine kinase (CK) and arginine kinase (AK). HTK is found only in sipunculid worms, and it shows activities for both the substrates hypotaurocyamine and taurocyamine. Determining how HTK evolved in sipunculids is particularly insightful because all sipunculid-allied animals have AK and only some sipunculids have HTK. We determined the cDNA sequence of HTK from the sipunculid worm Siphonosoma cumanense for the first time, cloned it in pMAL plasmid and expressed it in E. coli as a fusion protein with maltose-binding protein. The cDNAderived amino acid sequence of Siphonosoma HTK showed high amino acid identity with molluscan AKs. Nevertheless, the recombinant enzyme of Siphonosoma HTK showed no activity for the substrate arginine, but showed activity for taurocyamine. Comparison of the amino acid sequences of HTK and AK indicated that the amino acid residues necessary for the binding of the substrate arginine in AK have been completely lost in Siphonosoma HTK sequence. The phylogenetic analysis indicated that the HTK amino acid sequence was placed just outside the molluscan AK cluster, which formed a sister group with the arthropod and nematode AKs. These results suggest that Siphonosoma HTK evolved from a gene for molluscan AK. Moreover, to confirm this assertion, we determined by PCR that the gene for Siphonosoma HTK has a 5-exon/4-intron structure, which is homologous with that of the molluscan AK genes. Further, the positions of splice junctions were conserved exactly between the two genes. Thus, we conclude that Siphonosoma HTK has evolved from a primordial gene for molluscan AK.

show abstract

Section: Exon/intron Organization Of Siphonosoma Htk Gene Ismentioning

confidence: 94%

Hypotaurocyamine kinase evolved from a gene for arginine kinase

2005

Self Cite

View full text Add to dashboard Cite

show abstract

“…They showed that the domains are non-equivalent in terms of activity and that the extent of activity depends upon which combination of domain (s) Very recently, we have examined the properties of the "contiguous" dimeric AK from the sea anemone Anthopleula japonicus [Tada et al, 2008]. Anthopleula two-domain and Calyptogena two-domain AKs are enzymes which evolved independently in quite different lineages [Uda et al, 2006]. Tada et al (2008) were able to express the two-domain wild-type enzyme as well as individual domains 1 and 2.…”

Section: Are Both Of the Two Domains Of Two-domain Ak Active? Kineticmentioning

confidence: 99%

“…Members of this enzyme family play a key role in animals as ATP buffering systems in cells that display high and variable rates of ATP turnover [Kenyon and Reed, 1983;Wyss et al, 1992;Ellington, 2001]. AK is most widely distributed among organisms; its activity has been observed in arthropods, molluscs, nematoda, cnidarians, poriferae (the most ancient multi-cellular organisms), protozoans (ciliates, Trypanosoma and choanoflagellates) and bacteria [Watts and Bannister, 1970;Noguchi et al, 2001;Pereira et al, 2000;Uda et al, 2006;Conejo et al, 2008;Andrews et al, 2008], indicating an ancient origin of AK. Most AKs are monomers with a relative molecular mass of approximately 40 kDa [Morrison, 1973].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, deuterostome AKs and a unique AK from the polychaete Sabellastarte are part of this supercluster and appear to have evolved from an ancestral mitochondrial CK-like gene Tanaka et al, 2007]. The second super cluster consists of typical AKs distributed widely in animals and protozoans, and of a hypotaurocyamine kinase of sipunculids [Uda et al, 2006;Uda et al, 2005]. In contrast to the relatively conserved exon/intron organization in the genes of the CK cluster Tanaka et al, 2007], those of the AK cluster seem to be highly divergent, suggesting that a frequent loss or gain of introns has occurred during the course of AK evolution [Uda et al, 2006].…”

Section: Introductionmentioning

confidence: 99%

“…The second super cluster consists of typical AKs distributed widely in animals and protozoans, and of a hypotaurocyamine kinase of sipunculids [Uda et al, 2006;Uda et al, 2005]. In contrast to the relatively conserved exon/intron organization in the genes of the CK cluster Tanaka et al, 2007], those of the AK cluster seem to be highly divergent, suggesting that a frequent loss or gain of introns has occurred during the course of AK evolution [Uda et al, 2006]. It should be noted that during the course of AK evolution, unusual 80 kDa AKs evolved independently four times -in protozoa, cnidarians, plathyhelminths and heterodont clams.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Two-domain arginine kinase from the deep-sea clam Calyptogena kaikoi—Evidence of two active domains

Uda

Yamamoto

Iwasaki

et al. 2008

Comparative Biochemistry and Physiology Part B: Biochemistry an

Self Cite

View full text Add to dashboard Cite

show abstract

Synthesis of N_ω‐Phospho‐l‐arginine by Biocatalytic Phosphorylation of l‐Arginine

Schoenenberger¹,

Wszołek²,

Milesi³

et al. 2016

ChemCatChem

View full text Add to dashboard Cite

The Nω‐phospho‐l‐arginine energy‐buffering system is mainly present in invertebrates for regulating energy requirements when it is highly needed, such as in the flight muscles of an insect or when energy supply fluctuates, as in the medically important protozoa Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. The lack of availability of this important metabolite was due to a tedious chemical procedure, by which Nω‐phospho‐l‐arginine was prepared in over 5 reaction steps in a low yield. Therefore, we aimed at improving the synthetic methodology for the preparation of this important metabolite. As site‐ and enantioselective kinases have been very useful catalysts for biocatalytic phosphorylations in straightforward syntheses of phosphorylated metabolites, a stable and selective arginine kinase has been selected for the selective phosphorylation of l‐arginine. The Arg gene has been cloned and expressed in E. coli and a highly active arginine kinase has been prepared. A simple synthesis of Nω‐phospho‐l‐arginine has been developed by arginine kinase catalyzed phosphorylation of l‐arginine combined with the recycling of the phosphorylating agent ATP by using the phosphoenolpyruvate/pyruvate kinase system. After standard work‐up, the desired product Nω‐phospho‐l‐arginine was obtained in gram quantities and in one step.

show abstract

Evolution of the arginine kinase gene family

Cited by 93 publications

References 45 publications

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Two-domain arginine kinase from the deep-sea clam Calyptogena kaikoi—Evidence of two active domains

Synthesis of N_ω‐Phospho‐l‐arginine by Biocatalytic Phosphorylation of l‐Arginine

Contact Info

Product

Resources

About

Evolution of the arginine kinase gene family

Cited by 93 publications

References 45 publications

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Hypotaurocyamine kinase evolved from a gene for arginine kinase

Two-domain arginine kinase from the deep-sea clam Calyptogena kaikoi—Evidence of two active domains

Synthesis of Nω‐Phospho‐l‐arginine by Biocatalytic Phosphorylation of l‐Arginine

Contact Info

Product

Resources

About

Synthesis of N_ω‐Phospho‐l‐arginine by Biocatalytic Phosphorylation of l‐Arginine