Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues

David B. Rozema; Scott T. Phillips; C. Dale Poulter

doi:10.1021/ol990814o

Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues

David B. Rozema, Scott T. Phillips, C. Dale Poulter

Chemistry

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Formula presented Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.

Original language	English (US)
Pages (from-to)	815-817
Number of pages	3
Journal	Organic Letters
Volume	1
Issue number	5
DOIs	https://doi.org/10.1021/ol990814o
State	Published - Sep 9 1999

All Science Journal Classification (ASJC) codes

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/ol990814o

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title = "Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues",

abstract = "Formula presented Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.",

author = "Rozema, {David B.} and Phillips, {Scott T.} and Poulter, {C. Dale}",

year = "1999",

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journal = "Organic Letters",

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T1 - Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues

AU - Rozema, David B.

AU - Phillips, Scott T.

AU - Poulter, C. Dale

PY - 1999/9/9

Y1 - 1999/9/9

N2 - Formula presented Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.

AB - Formula presented Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.

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JO - Organic Letters

JF - Organic Letters

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ER -

Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues

Abstract

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