Mechanistic studies on prolyl-4-hydroxylase: the vitamin c requiring uncoupled oxidation-Reference-Cited by-同舟云学术

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Mechanistic studies on prolyl-4-hydroxylase: the vitamin c requiring uncoupled oxidation

Published:2000-07 Issue:14 Volume:10 Page:1511-1514
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Wu Min,Moon Hong-sik,Pirskanen Asta,Myllyharju Johanna,Kivirikko Kari I.,Begley Tadhg P.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference20 articles.

1. Kivirikko, K. I.; Myllylä, R.; Pihlajaniemi, T. In Post Translational Modification of Proteins; Harding, J.; Crabbe, M., Eds.; CRC: 1992; pp 1–51.

2. A stereochemical concept for the catalytic mechanism of prolylhydroxylase

3. Mechanism-Based Inactivation of the Human Prolyl-4-hydroxylase by 5-Oxaproline-Containing Peptides: Evidence for a Prolyl Radical Intermediate

4. Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites

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2. Beyond the Antioxidant: The Double Life of Vitamin C;Subcellular Biochemistry;2011-08-31

3. Prolyl 4-hydroxylase activity-responsive transcription factors: From hydroxylation to gene expression and neuroprotection;Frontiers in Bioscience;2008

4. Development of a convenient peptide-based assay for lysyl hydroxylase;Biopolymers;2007-07-03

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