Sites actifs de l'atp:arginine phosphotransférase

Pradel, Louise‐Anne; Kassab, Rhida; Regnouf, Françoise; Thoại, Nguyễn Văn

doi:10.1016/0926-6569(64)90214-7

Cited by 7 publications

(13 citation statements)

References 7 publications

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“…The nature of the starting material probably accounts for the comparatively low specific activity of arginine kinase in the crude extract of whole flies. This activity is up to 10 times lower than in other reported purification procedures of arthropod arginine kinase where muscle tissue alone instead of whole animals could be used [6,22,23]. A typical purification protocol is summarized in Table 2.…”

Section: Purification and Characterizationmentioning

confidence: 81%

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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Section: Purification and Characterizationmentioning

confidence: 81%

Properties of Arginine Kinase from Drosophila melanogaster

Wallimann

Eppenberger

1973

European Journal of Biochemistry

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“…Activity measurements were determined, as described previously [6,12], on suitable aliquots of tyrosyl modified protein samples which were diluted in 0.05M glycine-NaOH pH 8.6 (except for the o-acetyl enzyme) and incubated for 30 min a t 25 "C with 0.005 M dithiothreitol. X-Sulfenyl sulfonate arginine kinase was reduced in the same conditions and was used as a 10Oo/, activity control.…”

Section: Enzymes Assaysmentioning

confidence: 99%

Effects of Iodination and Acetylation of Tyrosyl Residues on the Activity and Structure of Arginine Kinase from Lobster Muscle

Fattoum

Kassab

Pradel

1971

European Journal of Biochemistry

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The iodination and 0-acetylation of tyrosyl residues in arginine kinase from lobster muscle (Homarus vulgaris) with iodine and N-acetylimidazole have been studied after reversible blocking of the thiol groups.The conversion of one tyrosyl residue to monoiodotyrosine, as measured by spectrotitration and by radioactive iodine labeling, resulted in a total loss of activity.The extent of the conformational changes occurring after nitration by tetranitromethane and iodination was studied by the optical rotary dispersion and the hydrogen-tritium exchange techniques.The functional properties of this tyrosyl residue were underlined by the inhibition of arginine kinase after o-acetylation and the ability of the modified protein to recover full activity upon tyrosyl de-o-acetylation with neutral hydroxylamine.The present investigation was initiated in an effort to collect more information about the importance of aromatic side chains in the catalytic activity and the structure of arginine kinase from lobster muscle. The tyrosyl residues have focused our special attention since we have found [l] that the interaction of this phosphagen kinase with its guanidine substrates as well as with some hydrophobic L-a-amino acids or specific -SH reagents could be visualized spectrally by the occurrence of a characteristic difference spectrum involving a blue shift of tyrosine a t 280 and 287nm and a hypochromic phase a t 239 nm; this latter spectral modification was shown t o be a result of the direct participation of the essential cysteinyl residue of the protein in the binding process [2]. This spectral data pointed out the possible proximity of functional sulfhydryl and tyrosyl groups in the enzyme active site.I n an earlier report [3] we studied the inactivation of arginine kinase by nitration of a single tyrosyl residue with the specific tyrosine reagent, tetranitromethane. On the basis of the results obtained concerning the immunochemical reactivity and optical rotary dispersion properties of the mononitrated protein, we concluded that a gross conformational change accompanied the complete inhibition of the enzyme observed. To extend and confirm these observations, we have examined, during the course of this study, the effect of the chemical modification of the tyrosyl residues in arginine b a s e with two other reagents : iodine and N-acetylimidazole. It Enzyme. Arginine kinase (EC 2.7.3.3).30 Eur. J. Bioehem., Vol. 22 has been shown that monoiodination of a single tyrosyl residue altered both the catalytic activity and the three-dimensional structure of the enzyme ; the importance of this critical tyrosyl side chain in the maintenance of the native conformation of arginine kinase was further illustrated by the reversible inhibition of the enzyme upon tyrosyl o-acetylation with N-acetylimidazole. A preliminary account of this work was presented [4]. EXPERIMENTAL PROCEDURE MATERIALSArginine kinase from lobster muscle Homarus vulgaris was prepared as previously described [5,6]. Its specific activity was about 240 unitslmg. Be...

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“…Similar relationships have also been found for the Mg2 + activation of creatine and L-arginine kinases. 4 ) Like the other guanidino kinases including guanidinoacetate kinase from N. coeca, 6) this enzyme was completely inhibited by low concentrations of such sulfhydryl-group-blocking agents as PCMB and DTNB, demonstrating the importance of thiol groups for the catalytic function.…”

Section: Discussionmentioning

confidence: 99%

“…The optimum pH (around pH 8.1) of this enzyme in the forward reaction was slighly lower than those of guanidino kinases. Perinereis guanidinoacetate kinase II was thought to be more thermostable than the enzyme from N. coeca, 6) judging from the optimum temperatures of each enzyme (Perinereis sp. : 35°C, N. coeca: 22°C).…”

Section: Discussionmentioning

confidence: 99%

Purification and Properties of Guanidinoacetate Kinase from a Polychaete,Perinereissp.

Shirokane¹,

Nakajima²,

Mizusawa³

1991

Agricultural and Biological Chemistry

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Guanidinoacetate kinase (ATP: guanidinoacetate N-phosphotransferase, EC 2.7.3.1) was extracted and purified to homogeneity from a polychaete, Perinereis sp., by ammonium sulfate fractionation and chromatographies with Butyl-Toyopearl 650C, Sephadex G-200, and DEAESephacel gels. Perinereis guanidinoacetate kinase was separated into two active fractions (I and II) by DEAE-Sephacel column chromatography, which had similar specific activities, and so some properties of guanidinoacetate kinase II (a major fraction) were investigated. The molecular weight of the enzyme was 90,000 on gel filtration and it was composed of two non-identical subunits (47,000 and 45,000). The enzyme showed optimum activity around pH 8.1 and was stable from pH 5.5 to 9.5 in the forward reaction. It was strictly specific for guanidinoacetate, and ATP was the most effective phosphoryl group donor for the forward reaction. The enzyme was activated by metal ions such as Mg2 + or Mn 2 + while Ca 2 + was 29% as active as Mg2 + • The Km values were 4.1 mM and 0.80 mM for guanidinoacetate and ATP, respectively. The enzyme activity was strongly inhibited by sulfhydryl-group-blocking agents, Hg2+, N-bromosuccinimide, and SDS. ADP and agmatine were competitive inhibitors.

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Sites actifs de l'atp:arginine phosphotransférase

Cited by 7 publications

References 7 publications

Properties of Arginine Kinase from Drosophila melanogaster

Properties of Arginine Kinase from Drosophila melanogaster

Effects of Iodination and Acetylation of Tyrosyl Residues on the Activity and Structure of Arginine Kinase from Lobster Muscle

Purification and Properties of Guanidinoacetate Kinase from a Polychaete,Perinereissp.

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