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H-Ras peptide and protein substrates bind protein farnesyltransferase as an ionized thiolate.

Abstract：

:The zinc metalloenzyme protein farnesyltransferase (FTase) catalyzes the alkylation of a cysteine residue of protein substrates with a 15 carbon farnesyl group. We have developed fluorescence assays to directly measure the affinity of the enzyme for peptide and protein (Ras) substrates. A peptide corresponding to the carboxyl terminus of H-Ras binds to FTase in the microM range (KD = 4 microM) at physiological pH; however, the peptide affinity is enhanced approximately 70-fold in a ternary complex with an enzyme-bound farnesyl diphosphate (FPP) analogue, indicating that the two substrates bind synergistically. The pH dependence of substrate binding was also investigated, and two ionizations were observed: for the ternary complex, the pKa values are 8.1, reflecting ionization of the thiol of the free peptide, and 6.4. The pH dependence of the ligand-metal charge-transfer band in the optical absorption spectra of a Co2+-substituted FTase ternary complex suggests that a metal-coordinated thiol ionizes with a pKa of 6.3. These data indicate that metal coordination of the peptide sulfur with the zinc ion in FTase lowers the pKa of the thiol resulting in formation of a bound thiolate at physiological pH.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Hightower KE,Huang CC,Casey PJ,Fierke CA

doi

10.1021/bi981525v

subject

Has Abstract

pub_date

1998-11-03 00:00:00

pages

15555-62

issue

44

eissn

0006-2960

issn

1520-4995

pii

bi981525v

journal_volume

37

pub_type

杂志文章

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