Direct photolabeling of the EcoRII methyltransferase with S-adenosyl-L-methionine.
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منابع مشابه
Biosynthesis of mycophenolic acid: purification and characterization of S-adenosyl-L-methionine: demethylmycophenolic acid O-methyltransferase.
The final step in the biosynthesis of mycophenolic acid involves the transfer of a methyl group from S-adenosylmethionine to demethylmycophenolic acid. The enzyme, S-adenosylmethionine:demethylmycophenolic acid O-methyltransferase, was isolated from Penicillium stoloniferum and purified 2,700-fold by ammonium sulfate fractionation and diethylaminoethyl-cellulose and Sephadex G-200 chromatograph...
متن کاملPurification, characterization, and molecular cloning of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Methanobacterium ivanovii.
An S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase (SUMT) activity has been identified in Methanobacterium ivanovii and was purified 4,500-fold to homogeneity with a 38% yield. The enzyme had an apparent molecular weight of 58,200 by gel filtration and consisted of two identical subunits of Mr 29,000, as estimated by gel electrophoresis under denaturing conditions. The Km value f...
متن کاملNucleotide Sequence of S-Adenosyl-l-Methionine: Magnesium Protoporphyrin Methyltransferase from Rhodobacter capsulatus.
It is generally believed that Chl and bacteriochlorophyll biosynthesis are evolutionarily related. This supposition is supported by the observation that the biosynthetic pathway for Chl a involves intermediates that are common with bacteriochlorophyll a biosynthesis (reviewed in ref. 7) and by the observation that light-independent reduction of protochlorophyllide to Chlide involves an enzyme c...
متن کاملThe enzymatic decomposition of S-adenosyl-L-methionine.
The role of S-adenosyl-n-methionine as a methyl donor has been investigated in mammalian systems (1) and in microbial metabolism (2-4). In addition, the compound is involved in the formation of spermidine from putrescine (5). Information concerning the stability of S-adenosylmethionine in various enzymatic systems is a necessary prerequisite for studies concerning its role in group transfer. In...
متن کاملPurification of rat liver S-adenosyl-L-methionine decarboxylase.
The amount of S-adenosyl-l-methionine decarboxylase present in rat liver was enhanced 17-fold by administration of methylglyoxal bis(guanylhydrazone),* a specific inhibitor of the enzyme. The enzyme was purified 1400-fold in 50% yield from such liver extracts by chromatography on columns of the inhibitor bound to Sepharose. The purified enzyme had no spermidine synthetase activity.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)39559-6