Results 131 to 140 of about 2,966 (173)
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Human liver prenyltransferase and its characterization
Biochimica Et Biophysica Acta - Biomembranes, 1981Prenyltransferase (dimethylallydiphosphate: isopentenyldiphosphate dimethylallytransferase, EC 2.5.1.1) has been purified to homogeneity from human liver obtained at autopsy. The enzyme is a dimer with a native molecular weight of 74 000 +/- 1 400. The amino acid composition is reported.
G Popják
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Reactivity of artificial substrates for prenyltransferase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Four compounds out of 6 new allylic pyrophosphates synthesized were found to act as artificial substrates for pig liver prenyltransferase (dimethylallylpyrophosphate:isopentenylpyrophosphate dimethylallyltransferase, EC 2.5.1.1). These were cyclopentylideneethyl, cyclohexylideneethyl, trans-3-ethyl-2-hexenyl, and cis-3-ethyl-2-hexenyl pyrophosphates. 2-
T, Nishino, K, Ogura, S, Seto
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Prenyltransferases of the Dimethylallyltryptophan Synthase Superfamily
2012Prenylated natural products often have interesting biological and pharmacological activities clearly distinct from their nonprenylated precursors. Prenyltransferases are responsible for the attachment of prenyl moieties to a number of acceptors and contribute significantly to structural and biological diversity of these compounds in nature. In the past
Xia, Yu, Shu-Ming, Li
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Mechanistic studies on the indole prenyltransferases
Natural Product Reports, 2015This review article presents a review of recent mechanistic studies on the reactions catalyzed by the soluble indole prenyltransferases.
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Substrate binding of avian liver prenyltransferase
Biochemistry, 1976Prenyltransferase (farnesyl pyrophosphate synthetase) was purified from avian liver and characterized by Sephadex and sodium dodecyl sulfate gel chromatography, peptide mapping, and end-group analysis. The enzyme is 85 800 +/- 4280 daltons and consists of two identical subunits as judged by sodium dodecyl sulfate gel electrophoresis, peptide mapping ...
B C, Reed, H C, Rilling
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Prenyltransferase Inhibitors as Radiosensitizers
2001Radiation therapy is frequently used in the treatment of a number of different tumors. However, the effectiveness of radiotherapy is limited by the ability of normal tissues adjacent to tumors to tolerate radiation in the doses required to kill or sterilize tumor cells.
Eric J. Bernhard +6 more
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Photoaffinity labeling of the catalytic site of prenyltransferase
Biochemistry, 1979Three photoreactive substrate analogues, o-azidophenethyl pyrophosphate, p-azidophenethyl pyrophosphate, and 3-azido-1-butyl pyrophosphate, have been synthesized as site-directed probes to label the catalytic site of prenyltransferase. Due to the relatively poor affinity of p-azidophenethyl pyrophosphate and 3-azido-1-butyl pyrophosphate for the enzyme,
D N, Brems, H C, Rilling
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Protein Prenyltransferases: Anchor Size, Pseudogenes and Parasites
Biological Chemistry, 2003Lipid modification of eukaryotic proteins by protein prenyltransferases is required for critical signaling pathways, cell cycle progression, cytoskeleton remodeling, induction of apoptosis and vesicular trafficking. This review analyzes the influence of distinct states of sequential posttranslational processing that can be obtained after single or ...
Maurer-Stroh, Sebastian +2 more
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[16] Eukaryotic prenyltransferases
1985Publisher Summary This chapter discusses the prenyltransferase of sterol biosynthesis in eukaryotes. This enzyme condenses either a C 5 or a C 10 allylic pyrophosphate with the homoallylic pyrophosphate to give, as the ultimate product, farnesyl pyrophosphate which then serves as a substrate for squalene and sterol synthesis.
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