Results 181 to 190 of about 3,663 (218)

Prenyltransferase from Gossypium hirsutum

Archives of Biochemistry and Biophysics, 1980
Abstract A protein fraction has been purified from Gossypium hirsutum var. Coker 413 which synthesized all four geometrical isomers of farnesyl pyrophosphate from isopentenyl pyrophosphate alone, from isopentenyl pyrophosphate and geranyl or neryl pyrophosphate. Electrophoretic analysis showed that this protein fraction consisted of three proteins.
R, Widmaier, J, Howe, P, Heinstein
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Prenyltransferases of the Dimethylallyltryptophan Synthase Superfamily

2012
Prenylated 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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Substrate binding of avian liver prenyltransferase

Biochemistry, 1976
Prenyltransferase (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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Photoaffinity labeling of the catalytic site of prenyltransferase

Biochemistry, 1979
Three 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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Mechanistic studies on the indole prenyltransferases

Natural Product Reports, 2015
This review article presents a review of recent mechanistic studies on the reactions catalyzed by the soluble indole prenyltransferases.
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Protein Prenyltransferases: Anchor Size, Pseudogenes and Parasites

Biological Chemistry, 2003
Lipid 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, Washietl, Stefan, Eisenhaber, Frank   +2 more
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Prenyltransferase Inhibitors as Radiosensitizers

2001
Radiation 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, Ruth J. Muschel, Elizabeth Cohen-Jonathan, Gilles Favre, Andrew D. Hamilton, Saïd M. Sebti, W. Gillies McKenna   +6 more
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[16] Eukaryotic prenyltransferases

1985
Publisher 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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CdpC2PT, a reverse prenyltransferase from Neosartorya fischeri with a distinct substrate preference from known C2-prenyltransferases

Microbiology, 2013
A putative prenyltransferase gene, NFIA_043650, was amplified from Neosartorya fischeri NRRL 181 and cloned into the expression vector pQE60. The deduced polypeptide consisting of 445 amino acids with a molecular mass of 51 kDa was overproduced in Escherichia coli and purified as His6-tagged protein to near homogeneity. The purified soluble protein was
Kathrin, Mundt, Shu-Ming, Li
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Prenylation of RAS and Inhibitors of Prenyltransferases

1996
The recent development of farnesyltransferase inhibitors which inhibit the growth of RAS-transformed cells demonstrates that membrane association of RAS and other monomeric G proteins such as Rho is important for the tumorigenicity of RAS.1–3 In the early 1980s, it was established that RAS is C-terminally modified and that this modification is ...
Isabel Sattler, Fuyuhiko Tamanoi
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