Selenophosphate synthetase. Enzyme properties and catalytic reaction.
نویسندگان
چکیده
منابع مشابه
Selenophosphate synthetase. Enzyme properties and catalytic reaction.
Selenophosphate synthetase, the product of the selD gene, produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide. Isolation of the enzyme and characterization of some of its physical and catalytic properties are described. Magnesium ion and a monovalent cation, K+, NH4+, or Rb+, are required for catalytic activity. Polyphosphates and other common nu...
متن کاملStructural insights into the catalytic mechanism of Escherichia coli selenophosphate synthetase.
Selenophosphate synthetase (SPS) catalyzes the synthesis of selenophosphate, the selenium donor for the biosynthesis of selenocysteine and 2-selenouridine residues in seleno-tRNA. Selenocysteine, known as the 21st amino acid, is then incorporated into proteins during translation to form selenoproteins which serve a variety of cellular processes. SPS activity is dependent on both Mg(2+) and K(+)...
متن کاملA Synthetase Reaction EVIDENCE FOR SUBSTRATE SYNERGISM AND CATALYTIC COOPERATIVITY
Escherichia coli succinyl-CoA synthetase has an a& structure (molecular weight, 140,000) with the two active sites arranged at the interface of the a and j3 subunits. Here we describe 31P-NMR experiments confirming the existence of two phosphorylated intermediates in catalysis. The phosphohistidyl resonance is readily observed at -4.8 ppm. This resonance is shifted upfield in the presence of M&...
متن کاملCystathionine y-Synthetase of SaZmoneZZa CATALYTIC PROPERTIES OF A NEW ENZYME IN BACTERIAL METHIONINE BIOSYNTHESIS
An enzyme catalyzing the synthesis of L-cystathionine from the succinyl ester of L-homoserine and L-cysteine was isolated from a Salmonella mutant blocked in another step of methionine synthesis, and derepressed for cystathionine y-synthetase formation. The approximate molecular weight of the enzyme was 155,000 and it was unchanged after removal of tightly bound pyridoxal phosphate. In the abse...
متن کاملCystathionine y-Synthetase of SaZmoneZZa CATALYTIC PROPERTIES OF A NEW ENZYME IN BACTERIAL METHIONINE BIOSYNTHESIS
An enzyme catalyzing the synthesis of L-cystathionine from the succinyl ester of L-homoserine and L-cysteine was isolated from a Salmonella mutant blocked in another step of methionine synthesis, and derepressed for cystathionine y-synthetase formation. The approximate molecular weight of the enzyme was 155,000 and it was unchanged after removal of tightly bound pyridoxal phosphate. In the abse...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34101-7