Detail of "10236-58-5"

Reference

Biology and biochemistry of selenium elements

Biology and biochemistry of selenium elements. Forchhammer, K.; Boeck, A. (Univ. Muenchen, Munich W-8000, Germany). Naturwissenschaften, 78(11), 497-504 (German) 1991. CODEN: NATWAY.There are some reagents with their cas registry numbers 7782-49-2 and 10236-58-5 are used in this study. ISSN: 0028-1042. DOCUMENT TYPE: Journal; General Review CA Section: 6 (General Biochemistry) Section cross-reference(s): 7, 17 A review and discussion with 42 refs., of the importance of Se as an essential trace element, which has progressively emerged during the last years due to the anal. of Se deficiency diseases and to the identification and characterization of a no. of selenoenzymes. Se is incorporated in the catalytic site of the enzymes as an integral selenocysteine residue. The pathway of selenocysteine biosynthesis and incorporation has been elucidated recently for Escherichia coli. The mechanisms which confer selenocysteine specificity in the framework of protein biosynthesis are described. In addn., some considerations concerning the phylogeny of selenocysteine incorporation are presented and a model for the evolution of the selenocysteine incorporation pathway is proposed. .

Sulfur metabolism in Paracoccus denitrificans

Sulfur metabolism in Paracoccus denitrificans. Purification, properties and regulation of cysteinyl- and methionyl-tRNA synthetase. Burnell, J. N.; Whatley, F. R. (Bot. Sch., Oxford, Engl.). Biochim. Biophys. Acta, 481(1), 266-78 (English) 1977. CODEN: BBACAQ. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 10 Cysteinyl- and methionyl-tRNA synthetases (I and II, resp. 10236-58-5 and 62817-80-5 which are cas registry numbers are also used here.) were purified 1200- and 1000-fold, resp., from sonic exts. of P. denitrificans strain 8944, and reaction kinetics, substrate specificity, and regulatory properties were detd. using the ATP-pyrophosphate exchange reaction. Both enzymes had pH optima of .apprx.8 and were inhibited by SH-group reagents. I catalyzed L-selenocysteine- and .alpha.-aminobutyric acid-dependent ATP-pyrophosphate exchange and II catalyzed L-homocysteine-, L-selenomethionine, and norleucine-dependent ATP-pyrophosphate exchange. Both enzymes were inhibited by O-acetylserine. I activity was stimulated by methionine and II activity was stimulated by sulfide, cysteine, and cysteic acid. .