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...
متن کاملControl of radical chemistry in the AdoMet radical enzymes.
The radical AdoMet superfamily comprises a diverse set of >2800 enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (SAM or AdoMet) to initiate a diverse set of radical-mediated reactions. The intricate control these enzymes exercise over the radical transformations they catalyze is an amazing feat of elegance and sophistication in biochemistry. This review focuses on the accumul...
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Ribonucleotide reductases catalyze a key step in DNA biosynthesis, using a diverse array of unprecedented metallo-cofactors to generate a transient protein radical that initiates nucleotide reduction. The new understanding of the chemistry and biochemistry of the system has allowed rational design of inhibitors of this process, which function as antitumor and antiviral agents.
متن کاملStructure and function of radical SAM enzymes.
'Radical SAM' enzymes juxtapose a [4Fe-4S] cluster and S-adenosyl-l-methionine (SAM) to generate catalytic 5'-deoxyadenosyl radicals. The crystal structures of oxygen-independent coproporphyrinogen III oxidase HemN and biotin synthase reveal the positioning of both cofactors with respect to each other and relative to the surrounding protein environment. Each is found in an unprecedented coordin...
متن کاملCrystallization Studies of 5'-deoxyadenosyl Radical Enzymes
ion from a cysteine thiol, which then catalyzes the reduction of ribonucleotides (Figure 1.3). While the overall mechanism of this reaction varies greatly from that of the isomerases, in every case, the reaction involves abstraction of a hydrogen atom by Ado*. 1.2.3. Adenosylcobalamin transport and activation For AdoCbl-dependent isomerases in the absence of substrate, the cobalamin homolysis p...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)81412-s