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분자활성 촉매반응 연구단
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A human protein hydroxylase that accepts D-residues

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Title
A human protein hydroxylase that accepts D-residues
Author(s)
Hwanho Choi; Adam P. Hardy; Thomas M. Leissing; Rasheduzzaman Chowdhury; Yu Nakashima; Wei Ge; Marios Markoulides; John S. Scotti; Philip A. Gerken; Helen Thorbjornsrud; Dahye Kang; Sungwoo Hong; Joongoo Lee; Michael A. McDonough; Hwangseo Park; Christopher J. Schofield
Publication Date
2020-05
Journal
COMMUNICATIONS CHEMISTRY, v.3, no.1, pp.52
Publisher
NATURE PUBLISHING GROUP
Abstract
© 2020, The Author(s), Factor inhibiting hypoxia-inducible factor (FIH) is a 2-oxoglutarate-dependent protein hydroxylase that catalyses C3 hydroxylations of protein residues. We report FIH can accept (D)- and (L)-residues for hydroxylation. The substrate selectivity of FIH differs for (D) and (L) epimers, e.g., (D)- but not (L)-allylglycine, and conversely (L)- but not (D)-aspartate, undergo monohydroxylation, in the tested sequence context. The (L)-Leu-containing substrate undergoes FIH-catalysed monohydroxylation, whereas (D)-Leu unexpectedly undergoes dihydroxylation. Crystallographic, mass spectrometric, and DFT studies provide insights into the selectivity of FIH towards (L)- and (D)-residues. The results of this work expand the potential range of known substrates hydroxylated by isolated FIH and imply that it will be possible to generate FIH variants with altered selectivities
URI
https://pr.ibs.re.kr/handle/8788114/8626
DOI
10.1038/s42004-020-0290-5
ISSN
2399-3669
Appears in Collections:
Center for Catalytic Hydrocarbon Functionalizations(분자활성 촉매반응 연구단) > 1. Journal Papers (저널논문)
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