The 2-Oxoglutarate-Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5S-Hydroxylysine Residues

被引：52

作者：

Mantri, Monica ^{[1
]}

Loik, Nikita D. ^{[1
]}

Hamed, Refaat B. ^{[1
,2
]}

Claridge, Timothy D. W. ^{[1
]}

McCullagh, James S. O. ^{[1
]}

Schofield, Christopher J. ^{[1
]}

机构：

[1] Univ Oxford, Dept Chem, Oxford OX1 3TA, England

[2] Assiut Univ, Dept Pharmacognosy, Fac Pharm, Assiut 71256, Egypt

来源：

CHEMBIOCHEM | 2011年 / 12卷 / 04期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

collagen; conformation analysis; enzyme catalysis; JMJD6; lysyl hydroxylation; HYPOXIA-INDUCIBLE FACTOR; DOMAIN-CONTAINING PROTEINS; ANKYRIN REPEAT DOMAIN; ASPARAGINYL HYDROXYLATION; HISTONE DEMETHYLASES; AMINO-ACIDS; CHROMATOGRAPHY; FIH;

D O I：

10.1002/cbic.201000641

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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页码：531 / 534

页数：4

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