Phosphagen Kinases and Evolution in the Echinodermata

Moreland, Barbara H.; Watts, D C; Virden, Richard

doi:10.1038/214458a0

Cited by 60 publications

(12 citation statements)

References 29 publications

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“…Arginine kinase occurs in monomeric and dimeric forms in a wide range of invertebrate organisms (Moreland et al, 1967). Many invertebrates contain other phosphagens, which can function as substrates for phosphotransferases, although vertebrate kinases appear to be limited to creatine as the phosphate acceptor (Ellington, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Mg ATP + L-arginine º MgADP + L-arginine phosphate + H + The enzyme is widely distributed among invertebrates (Moreland et al, 1967) and is functionally analogous to the more thoroughly studied creatine kinase found in vertebrates (Watts, 1973). These phosphagen kinases may directly (Bessman and Geiger, 1981) or indirectly (Ouellet and Shoubridge, 1992) regulate availability of ATP.…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of arginine kinase from the American cockroach (Periplaneta americana)

Brown

FRANCE

Grossman

2004

Arch Insect Biochem Physiol

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The isolation and characterization of homogeneous arginine kinase from the cockroach is reported. The purification protocol produces 6.6 mg of pure enzyme from 6.8 g of whole cockroach. The purified enzyme cross-reacts with a heterologous antibody and monoclonal antibody against arginine kinase from the shrimp. Both antibody preparations also cross-react with extracts from several species known to contain monomeric arginine kinase, but fail to react with extracts from organisms containing dimeric arginine kinase. Cockroach arginine kinase has a molecular mass of approximately 43,000 determined from measurements by gel filtration and gel electrophoresis. Compared with other arginine kinases, the enzyme from the cockroach is relatively thermostable (50% activity retained at 50 degrees C for 10 min) and has a pH optima of 8.5 and 6.5-7.5, for the forward and reverse reactions, respectively. Treatment with 5,5'dithiobis[2-nitrobenzoic acid] indicates that arginine kinase has a single reactive sulfhydryl group and, interestingly, the reaction is biphasic. The Michaelis constants for the phosphagen substrates, arginine: 0.49 mM, phosphoarginine: 0.94 mM, and nucleotide substrates MgATP: 0.14 mM, MgADP: 0.09 mM, are in the range reported for other arginine kinases. A 1% solution of pure enzyme has an absorbance of 7.0 at 280 nm. Calculations based on circular dichroic spectra indicate that arginine kinase from the cockroach has 12% alpha-helical structure. The intrinsic protein fluorescence emission maximum at 340 nm suggests that tryptophan residues are below the surface of the protein and not exposed to solvent. Arginine kinase from the cockroach and shrimp are known to be deleterious immunogens towards humans. The availability of pure protein, its characterization and potential regulation of activity, will be useful in developing agents to control the cockroach population and its destructive role in agriculture and human health.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Purification and characterization of arginine kinase from the American cockroach (Periplaneta americana)

Brown

FRANCE

Grossman

2004

Arch Insect Biochem Physiol

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“…Arginine kinases from several echinoderms and molluscs have been found to be dimeric molecules, with molecular weights of approximately 80000 [4,5].…”

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confidence: 99%

Properties of Arginine Kinase from Drosophila melanogaster

Wallimann

Eppenberger

1973

European Journal of Biochemistry

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1. Starch‐gel electrophoresis of extracts of several strains of the genus Drosophila reveals neither allelic variants nor isoenzymes of arginine kinase. Arginine kinase of the drosophilid Zaprionus vittiger migrates differently. 2. Arginine kinase is non‐uniformly distributed in tissues of Drosophila melanogaster. The activity in muscle tissue represents about 70% of the total activity. A characteristic fluctuation of the enzyme activity during the development from the egg to the adult stage can be observed. 3. Purification of arginine kinase of Drosophila melanogaster has been achieved. Several physico‐chemical properties of the enzyme have been determined. The molecular weight in the range of 40 000 is comparable to other arthropod arginine kinases and suggests that the active enzyme is a monomer.

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“…However, all previous determinations of the quaternary structure of the phosphagen kinases were carried out on protein molecules of molecular weight 40000 or 80000, which is the usual size for these enzymes. Exceptionally, a creatine kinase of molecular weight 150 000 -175 000 had been found in the lantern muscle of an echinoderm, Echinus esculentus [8], and an arginine kinase of molecular weight 150000 -160000 had been characterized in the body-wall muscle of a sabellid worm closely related to Subeflu pavonina, Spirogruphis spallunzanii [2]. Their molecular weights were compatible with the existence of tetramers, but their subunit structure had not been further investigated.…”

Section: Discussionmentioning

confidence: 99%

Unspecific Arginine Kinase of Molecular Weight 150000. Amino Acid Composition, Subunit Structure and Number of Substrate Binding Sites

Robin¹,

Guillou²,

Thoại³

1975

European Journal of Biochemistry

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The amino acid composition of unspecific arginine kinase of molecular weight 150000 of Sabella pavonina muscle has been determined. It was found to be very similar to that of the phosphagen kinases previously studied.The subunit structure of the enzyme has been investigated by physical and chemical means.The data obtained from ultracentrifugation studies in 6 M guanidine hydrochloride and from molecular sieving and disc electrophoresis in 8 M urea, as well as the tryptic peptide mapping, suggest that Sabella muscle arginine kinase is composed of four non-covalently linked polypeptide chains, with similar molecular weights. The number of binding sites for the nucleotide substrate ADP-MgZ' has been estimated, using differential spectrophotometry and gel filtration on Sephadex columns. By both methods it was demonstrated that the enzyme contains two catalytic sites per protein molecule of molecular weight 150 000.Thus, arginine kinase from Sabella muscle, of molecular weight 150000, consists of four similar polypeptide chains, but possesses only two substrate binding sites per tetrameric molecule.The purification and some properties of a new molecular form of arginine kinase, isolated from the body-wall muscle of the marine annelid, Sabella pavanina, have been reported earlier [ l ] . The most interesting features of the enzyme were its molecular weight around 150000 [1,2], which is two or four times that of the invertebrate arginine kinases studied previously [3-101, and its comparatively wide specificity towards the guanidine substrates, especially towards the L and D forms of arginine [1,2, 111, in contrast with the strict specificity of most arginine kinases for L-arginine [11 -131.The present work is concerned with the study of the amino acid composition of the new enzyme, with the investigation of its quaternary structure by physical and chemical methods, and with the determination of the number of binding sites for the nucleotide substrate ADP-Mg2+. The results show that, in spite of significant differences in the molecular size and in the ratio of number of catalytic sites to number of subunits per enzyme molecule, several structural similarities can be pointed out between Sabella muscle arginine kinase and other muscle phosphagen kinases. EXPERIMENTAL PROCEDURE MaterialsSabella muscle arginine kinase was prepared as described previously [l], using ultrafiltration in a Diaflo cell (Amicon) fitted with a PM-30 membrane instead of Lyphogel, for the concentration of the protein solutions. The enzyme is labile and was utilized within 24 h following the last purification step, the final precipitation with ammonium sulfate being omitted and the enzyme being brought to a protein concentration of 5 to 10 mg/ml by ultrafiltration. Unspecific Arginine Kinase of Molecular Weight 150000 grade) and egg albumin (B grade) were from Calbiochem, trypsin (treated with N,N-dicyclohexyl carbodiimide) from Miles. Urea (Merck) was purified according to Poulik [16]. Guanidine hydrochloride RP from Carlo Erba was used without fur...

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Phosphagen Kinases and Evolution in the Echinodermata

Cited by 60 publications

References 29 publications

Purification and characterization of arginine kinase from the American cockroach (Periplaneta americana)

Purification and characterization of arginine kinase from the American cockroach (Periplaneta americana)

Properties of Arginine Kinase from Drosophila melanogaster

Unspecific Arginine Kinase of Molecular Weight 150000. Amino Acid Composition, Subunit Structure and Number of Substrate Binding Sites

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