Bioavailable affinity label for collagen prolyl 4-hydroxylase

JD Vasta, JJ Higgin, EA Kersteen, RT Raines

Index: Vasta, James D.; Higgin, Joshua J.; Kersteen, Elizabeth A.; Raines, Ronald T. Bioorganic and Medicinal Chemistry, 2013 , vol. 21, # 12 p. 3597 - 3601

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Citation Number: 3

Abstract

Collagen is the most abundant protein in animals. Its prevalent 4-hydroxyproline residues contribute greatly to its conformational stability. The hydroxyl groups arise from a post- translational modification catalyzed by the nonheme iron-dependent enzyme, collagen prolyl 4-hydroxylase (P4H). Here, we report that 4-oxo-5, 6-epoxyhexanoate, a mimic of the α-ketoglutarate co-substrate, inactivates human P4H. The inactivation installs a ketone ...