Structure-function studies of human aromatase by site-directed mutagenesis: kinetic properties of mutants Pro-308----Phe, Tyr-361----Phe, Tyr-361----Leu, and Phe-406----Arg.

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Structure-function studies of human aromatase by site-directed mutagenesis: kinetic properties of mutants Pro-308----Phe, Tyr-361----Phe, Tyr-361----Leu, and Phe-406----Arg.

Aromatase, a cytochrome P450, catalyzes the formation of aromatic C-18 estrogenic steroids from C-19 androgens. Four mutants of human aromatase have been expressed in Chinese hamster ovary cells using a stable expression method. The activities of these mutants were determined using [1 beta,2 beta-3H]androstenedione, [19-14C]androstenedione, and [1 beta,2 beta-3H]testosterone as substrates. The ...

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Neuropeptides Gly-Asp-Pro-Phe-Leu-Arg-Phe-amide (GDPFLRFamide) and Ser-Asp-Pro-Phe-Leu-Arg-Phe-amide (SDPFLRFamide) Are Encoded by an Exon 3’ to Phe-Met-Arg-Phe- NH, (FMRFamide) in the Snail Lymnaea stagnalis

Biochemical analysis has shown the pond snail Lymnaea stagnalis to contain 2 main classes of Phe-Met-Arg-Phe-NH, (FMRFamide)-like neuropeptides: the tetrapeptides FMRFamide and Phe-Leu-Arg-Phe-NH, (FLRFamide), and the heptapeptides Gly-Asp-Pro-Phe-Leu-Arg-Phe-NH, (GDPFLRFamide) and Ser-Asp-Pro-Phe-Leu-Arg-Phe-NH, (SDPFFRFamide). By genomic mapping and DNA sequencing, we show here that the GDP/S...

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Opioid receptor binding characteristics and structure-activity studies of novel tetrapeptides in the TIPP (Tyr-Tic-Phe-Phe) series.

The development of the prototype synthetic delta-opioid receptor antagonist peptides TIPP [(H-Tyr-Tic-Phe- Phe-OH); Tic: tetrahydroisoquinoline-3-carboxylic acid] and TIPPpsi (H-Tyr-psiTic-Phe-Phe-OH) by Schiller and coworkers was followed by extensive structure-activity relationship studies, leading to the emergence of numerous analogs that are of pharmacological interest. Eight novel diastere...

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Infinite pleated -sheet formed by the -hairpin Boc- -Phe- -Phe-D-Pro-Gly- -Phe- -Phe-OMe

A -hairpin conformation and extended -pleated sheet assembly have been characterized by single crystal x-ray diffraction for the synthetic peptide t-butoxycarbonyl— -Phe-Phe-D-Pro-GlyPhe-Phe-methyl ester [ -Phe: (S)3 homophenylalanine]. The centrally located D-Pro-Gly segment nucleates a chain reversal in a type II -turn conformation. Two intramolecular cross-strand hydrogen bonds stabilize the...

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Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin.

Investigations determined the mechanism(s) by which Arg-Pro-Pro-Gly-Phe (RPPGF) inhibits thrombin-induced platelet activation. High concentrations of RPPGF inhibit thrombin-induced coagulant activity. RPPGF binds to the active site of thrombin by forming a parallel beta-strand with Ser214-Gly216 and interacts with His57, Asp189, and Ser195 of the catalytic triad. RPPGF competitively inhibits al...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1991

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.88.2.410