Novel cofactors via post-translational mocifications of enzyme active sites

Nicole M. Okeley; Wilfred A. Van Der Donk

doi:10.1016/S1074-5521(00)00140-X

Novel cofactors via post-translational mocifications of enzyme active sites

Nicole M. Okeley, Wilfred A. Van Der Donk

Research output: Contribution to journal › Review article › peer-review

Abstract

Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.

Original language	English (US)
Pages (from-to)	R159-R171
Journal	Chemistry and Biology
Volume	7
Issue number	7
DOIs	https://doi.org/10.1016/S1074-5521(00)00140-X
State	Published - Jul 1 2000

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Clinical Biochemistry

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10.1016/S1074-5521(00)00140-X

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title = "Novel cofactors via post-translational mocifications of enzyme active sites",

abstract = "Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.",

author = "Okeley, {Nicole M.} and {Van Der Donk}, {Wilfred A.}",

note = "Funding Information: Research on post-translational modifications in the laboratory of W.A.V. is supported by the National Institutes of Health (GM5882) and the Burroughs-Wellcome Fund (APP 1920). N.M.O. gratefully acknowledges a pre-doctoral fellowship from Abbott Laboratories.",

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AU - Okeley, Nicole M.

AU - Van Der Donk, Wilfred A.

N1 - Funding Information: Research on post-translational modifications in the laboratory of W.A.V. is supported by the National Institutes of Health (GM5882) and the Burroughs-Wellcome Fund (APP 1920). N.M.O. gratefully acknowledges a pre-doctoral fellowship from Abbott Laboratories.

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N2 - Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.

AB - Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.

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Novel cofactors via post-translational mocifications of enzyme active sites

Abstract

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