DC Field | Value | Language |
---|---|---|
dc.contributor.author | Choi, Hwanho | ko |
dc.contributor.author | Hardy, Adam P. | ko |
dc.contributor.author | Leissing, Thomas M. | ko |
dc.contributor.author | Chowdhury, Rasheduzzaman | ko |
dc.contributor.author | Nakashima, Yu | ko |
dc.contributor.author | Ge, Wei | ko |
dc.contributor.author | Markoulides, Marios | ko |
dc.contributor.author | Scotti, John S. | ko |
dc.contributor.author | Gerken, Philip A. | ko |
dc.contributor.author | Thorbjornsrud, Helen | ko |
dc.contributor.author | Kang, Dahye | ko |
dc.contributor.author | Hong, Sungwoo | ko |
dc.contributor.author | Lee, Joongoo | ko |
dc.contributor.author | McDonough, Michael A. | ko |
dc.contributor.author | Park, Hwangseo | ko |
dc.contributor.author | Schofield, Christopher J. | ko |
dc.date.accessioned | 2020-05-27T01:20:18Z | - |
dc.date.available | 2020-05-27T01:20:18Z | - |
dc.date.created | 2020-05-25 | - |
dc.date.created | 2020-05-25 | - |
dc.date.created | 2020-05-25 | - |
dc.date.created | 2020-05-25 | - |
dc.date.issued | 2020-05 | - |
dc.identifier.citation | COMMUNICATIONS CHEMISTRY, v.3, no.1 | - |
dc.identifier.issn | 2399-3669 | - |
dc.identifier.uri | http://hdl.handle.net/10203/274316 | - |
dc.description.abstract | Hypoxia-inducible factor (FIH) is an oxygenase which post-translationally hydroxylates proteins and is implicated in a range of biological processes. Here a wide substrate tolerance for FIH is demonstrated, including for d-amino acids, where double hydroxylation of d-leucine is observed. 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. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | A human protein hydroxylase that accepts D-residues | - |
dc.type | Article | - |
dc.identifier.wosid | 000531309700001 | - |
dc.identifier.scopusid | 2-s2.0-85084154662 | - |
dc.type.rims | ART | - |
dc.citation.volume | 3 | - |
dc.citation.issue | 1 | - |
dc.citation.publicationname | COMMUNICATIONS CHEMISTRY | - |
dc.identifier.doi | 10.1038/s42004-020-0290-5 | - |
dc.contributor.localauthor | Hong, Sungwoo | - |
dc.contributor.nonIdAuthor | Choi, Hwanho | - |
dc.contributor.nonIdAuthor | Hardy, Adam P. | - |
dc.contributor.nonIdAuthor | Leissing, Thomas M. | - |
dc.contributor.nonIdAuthor | Chowdhury, Rasheduzzaman | - |
dc.contributor.nonIdAuthor | Nakashima, Yu | - |
dc.contributor.nonIdAuthor | Ge, Wei | - |
dc.contributor.nonIdAuthor | Markoulides, Marios | - |
dc.contributor.nonIdAuthor | Scotti, John S. | - |
dc.contributor.nonIdAuthor | Gerken, Philip A. | - |
dc.contributor.nonIdAuthor | Thorbjornsrud, Helen | - |
dc.contributor.nonIdAuthor | Lee, Joongoo | - |
dc.contributor.nonIdAuthor | McDonough, Michael A. | - |
dc.contributor.nonIdAuthor | Park, Hwangseo | - |
dc.contributor.nonIdAuthor | Schofield, Christopher J. | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | ANKYRIN REPEAT DOMAIN | - |
dc.subject.keywordPlus | ASPARAGINYL HYDROXYLASE | - |
dc.subject.keywordPlus | 2-OXOGLUTARATE-DEPENDENT OXYGENASES | - |
dc.subject.keywordPlus | BETA-HYDROXYLATION | - |
dc.subject.keywordPlus | HYPOXIA | - |
dc.subject.keywordPlus | TRANSLATION | - |
dc.subject.keywordPlus | DIOXYGENASE | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | SYNTHASE | - |
dc.subject.keywordPlus | ENZYMES | - |
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