Kinetic mechanism of isoprenylated protein methyltransferase.

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Kinetic mechanism of isoprenylated protein methyltransferase.

The kinetic mechanism of the rod outer segment (ROS) isoprenylated protein methyltransferase was investigated. This S-adenosyl-L-methionine (AdoMet)-linked enzyme transfers methyl groups to carboxyl-terminal isoprenylated cysteine residues of proteins, generating methyl esters. The enzyme also processes simple substrates such as N-acetyl-S-farnesyl-L-cysteine (L-AFC). Initial studies showed tha...

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Protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and dimethylation of peptidyl arginine residues. Although all PRMTs produce monomethyl arginine (MMA), type 1 PRMTs go on to form asymmetrically dimethylated arginine (ADMA), while type 2 enzymes form symmetrically dimethylated arginine (SDMA). PRMT1 is the major type 1 PRMT in vivo, thus it is the pri...

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Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6).

The protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the mono- and dimethylation of arginine residues in a variety of proteins. Although these enzymes play important roles in a variety of cellular processes, aberrant PRMT activity is associated with several disease states, including heart disease and cancer. In an effort to guide the development of inhibitors ta...

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Kinetic Mechanism and Inhibitory Study of Protein Arginine Methyltransferase 1

Protein arginine methyltransferase 1 (PRMT1) is a key posttranslational modification enzyme that catalyzes the methylation of specific arginine residues in histone and nonhistone protein substrates, regulating diverse cellular processes such as transcriptional initiation, RNA splicing, DNA repair, and signal transduction. Recently the essential roles of PRMT1 in cancer and cardiovascular compli...

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Characterization of the Product Specificity and Kinetic Mechanism of Protein Arginine Methyltransferase 1

Protein arginine methyltransferases (PRMTs) aid in the regulation of many biological processes by methylating specific arginyl groups within targeted proteins. The varied nature of the response to methylation is, in part, due to the diverse product specificity displayed by the PRMTs. In addition to site location within a protein, biological response is also determined by the degree (mono/dimeth...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1992

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)50125-9