Substrate-Dependent Cleavage Site Selection by Unconventional Radical S-Adenosylmethionine Enzymes in Diphthamide Biosynthesis
نویسندگان
چکیده
منابع مشابه
Radical S-Adenosylmethionine Enzymes
ing a H-atom from substrate. These and other kinetics studies demonstrated that PFL-AE could undergo multiple turnover events, with the 150 PFL activations per PFL-AE reported in Table 1 not the upper limit, but rather a number limited by the PFL:PFL-AE ratio in the steady-state kinetics assays. As can be seen from the data summarized in Table 1, PFL-AE is one of the few radical SAM enzymes dem...
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Sulfatases are a major group of enzymes involved in many critical physiological processes as reflected by their broad distribution in all three domains of life. This class of hydrolases is unique in requiring an essential post-translational modification of a critical active-site cysteine or serine residue to C(alpha)-formylglycine. This modification is catalyzed by at least three nonhomologous ...
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A [4Fe-4S](+) cluster reduces a bound S-adenosylmethionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical (5'-dA(•)). This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes. The strongly oxidizing 5'-dA(•) is quenched by abstracting a H-atom from a target species. In some cases, this species is an exogenous molecule of substra...
متن کاملSPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes.
S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate isomerase (TIM) barrel fold with N- and C-terminal extensions that tailor the structure of the enzyme to its specific function. One extension, termed a SPASM domain, binds two auxiliary [4Fe-4S] clusters and is present wi...
متن کاملThe biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.
Sulfur atoms are present as thiol and thioether functional groups in amino acids, coenzymes, cofactors, and various products of secondary metabolic pathways. The biosynthetic pathways for several sulfur-containing biomolecules require the substitution of sulfur for hydrogen at unreactive aliphatic or electron-rich aromatic carbon atoms. Examples discussed in this review include biotin, lipoic a...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2017
ISSN: 0002-7863,1520-5126
DOI: 10.1021/jacs.7b01712