Biogenese de deux guanidines soufrees: La taurocyamine et l'hypotaurocyamine

Thoại, Nguyễn Văn; Zappacosta, Serafino; Robin, Y

doi:10.1016/0010-406x(63)90035-5

Cited by 17 publications

(5 citation statements)

References 21 publications

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“…In other words, many invertebrates appear to have some type of transamidinase activity in which the amidine acceptor is not glycine and the product formed is not guanidinoacetate. Other investigators have reported that arginine-H2N-R amidinotransferases participate in biosynthesis of various guanidinium compounds: taurocyamine in various annelids (Thoai et al, 1963); lombricine in the earthworm (Rossiter et al, 1960); and streptomycin in Streptomyces griseus (Walker, 1958). The value of the phosphoryl derivatives of the various guanidine compounds, called phosphagens, to the organism has been discussed (Ennor & Morrison, 1958).…”

Section: Discussionmentioning

confidence: 99%

Distribution of creatine, guanidinoacetate and the enzymes for their biosynthesis in the animal kingdom. Implications for phylogeny

Pilsum

Stephens

Taylor

1972

Biochemical Journal

101

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1. The distribution of creatine and the creatine-synthesizing enzymes in the animal kingdom has been investigated. Creatine was found in tissues of all vertebrates examined, and in various invertebrates from phyla Annelida, Echinodermata, Hemichordata and Chordata, subphylum Cephalochordata. The activities of the creatine-synthesizing enzymes, arginine–glycine transamidinase and guanidinoacetate methylpherase, were not detected in the hagfish or in any of the invertebrates, including those in which creatine was found, with the exception that transamidinase activities were detected in the amphioxus and salt water clam; however, these activities are considered to be artifacts for reasons mentioned in the text. Additional evidence that the hagfish and various creatine-containing invertebrates could not synthesize creatine was the observation that these animals did not convert one or the other of the likely precursors of creatine (arginine and glycine) into creatine, in vivo. Further, the inability of these animals to synthesize creatine is correlated with the observations that all animals tested were able to abstract creatine from their aqueous environment. 2. The activities of the creatine-synthesizing enzymes were detected in the sea lamprey and in all but a few of the other vertebrates examined. Neither activity could be detected in the sharks and rays (cartilaginous fish), buffalo fish (bony fish) or the snapping turtle. Transamidinase or guanidinoacetate methylpherase activity could not be found in the salamander or garter snake, respectively. 3. The results obtained with the lamprey are in direct contrast with those obtained with the hagfish (both subphylum Agnatha, class Cyclostomata). The lamprey had the ability to synthesize creatine and did not abstract creatine from lake water. The hagfish did not have any apparent ability to synthesize creatine and did abstract creatine from sea water. The present report thus supports the theory that the myxinoid (hagfish) and petromyzoid (lamprey) agnathans are only distantly related. 4. The lack of creatine-synthesizing enzyme activities in the cartilaginous fishes may have phylogenetic significance, but may also be explained by the availability of creatine in the diet of these animals. The lack of one or both enzyme activities in vertebrates other than the hagfish and the cartilaginous fish is suggested to be the result of creatine in the diet.

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Section: Discussionmentioning

confidence: 99%

Distribution of creatine, guanidinoacetate and the enzymes for their biosynthesis in the animal kingdom. Implications for phylogeny

Pilsum

Stephens

Taylor

1972

Biochemical Journal

101

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“…In the former, taurocyamine results from the transamidination of taurine from arginine, as was shown by in vivo (Thoai et al, 1956c;Mori et al, 1981a) and in vitro (Shindo and Mori, 1980) studies in the rat. On the other hand, in vivo and in vitro studies have established that taurocyamine is formed in marine worms by oxidation of the sulfinic analogue, hypotaurocyamine (Thoai et al, 1963b).…”

Section: Sulfonic and Sulfinic Acidsmentioning

confidence: 99%

“…Hypotaurocyamine is formed in worms by transamidination from arginine; subsequent oxidation yields taurocyamine (Thoai et al , 1963b). The transamidination reaction seems to take place in preference in the gut and the oxidation of the sulfinic to sulfonic group in the muscle.…”

Section: Sulfonic and Sulfinic Acidsmentioning

confidence: 99%

Natural Guanidino Compounds

Robin¹,

Marescau

1985

Guanidines

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“…TK was first isolated from the body wall muscle of polychaete lugworm Arenicola marina [17,18]. It shows considerable activity for hypotaurocyamine (about 50% of that of the main target substrate, taurocyamine), and weak activity for lombricine and glycocyamine [19].…”

mentioning

confidence: 99%

Origin and properties of cytoplasmic and mitochondrial isoforms of taurocyamine kinase

et al. 2005

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Taurocyamine kinase (TK) is a member of the highly conserved family of phosphagen kinases that includes creatine kinase (CK) and arginine kinase. TK is found only in certain marine annelids. In this study we used PCR to amplify two cDNAs coding for TKs from the polychaete Arenicola brasiliensis, cloned these cDNAs into the pMAL plasmid and expressed the TKs as fusion proteins with the maltose-binding protein. These are the first TK cDNA and deduced amino acid sequences to be reported. One of the two cDNA-derived amino acid sequences of TKs shows a high amino acid identity to lombricine kinase, another phosphagen kinase unique to annelids, and appears to be a cytoplasmic isoform. The other sequence appears to be a mitochondrial isoform; it has a long N-terminal extension that was judged to be a mitochondrial targeting peptide by several on-line programs and shows a higher similarity in amino acid sequence to mitochondrial creatine kinases from both vertebrates and invertebrates. The recombinant cytoplasmic TK showed activity for the substrates taurocyamine and lombricine (9% of that of taurocyamine). However, the mitochondrial TK showed activity for taurocyamine, lombricine (30% of that of taurocyamine) and glycocyamine (7% of that of taurocyamine). Neither TK catalyzed the phosphorylation of creatine. Comparison of the deduced amino acid sequences of mitochondrial CK and TK indicated that several key residues required for CK activity are lacking in the mitochondrial TK sequence. Homology models for both cytoplasmic and mitochondrial TK, constructed using CK templates, provided some insight into the structural correlation of differences in substrate specificity between the two TKs. A phylogenetic analysis using amino acid sequences from a broad spectrum of phosphagen kinases showed that annelid-specific phosphagen kinases (lombricine kinase, glycocyamine kinase and cytoplasmic and mitochondrial TKs) are grouped in one cluster, and form a sister-group with CK sequences from vertebrate and invertebrate groups. It appears that the annelid-specific phosphagen kinases, including cytoplasmic and mitochondrial TKs, evolved from a CK-like ancestor(s) early in the divergence of the protostome metazoans. Furthermore, our results suggest that the cytoplasmic and mitochondrial isoforms of TK evolved independently.Abbreviations

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Biogenese de deux guanidines soufrees: La taurocyamine et l'hypotaurocyamine

Cited by 17 publications

References 21 publications

Distribution of creatine, guanidinoacetate and the enzymes for their biosynthesis in the animal kingdom. Implications for phylogeny

Distribution of creatine, guanidinoacetate and the enzymes for their biosynthesis in the animal kingdom. Implications for phylogeny

Natural Guanidino Compounds

Origin and properties of cytoplasmic and mitochondrial isoforms of taurocyamine kinase

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