A human protein hydroxylase that accepts D-residues

Cited 6 time in webofscience Cited 4 time in scopus
  • Hit : 478
  • Download : 228
DC FieldValueLanguage
dc.contributor.authorChoi, Hwanhoko
dc.contributor.authorHardy, Adam P.ko
dc.contributor.authorLeissing, Thomas M.ko
dc.contributor.authorChowdhury, Rasheduzzamanko
dc.contributor.authorNakashima, Yuko
dc.contributor.authorGe, Weiko
dc.contributor.authorMarkoulides, Mariosko
dc.contributor.authorScotti, John S.ko
dc.contributor.authorGerken, Philip A.ko
dc.contributor.authorThorbjornsrud, Helenko
dc.contributor.authorKang, Dahyeko
dc.contributor.authorHong, Sungwooko
dc.contributor.authorLee, Joongooko
dc.contributor.authorMcDonough, Michael A.ko
dc.contributor.authorPark, Hwangseoko
dc.contributor.authorSchofield, Christopher J.ko
dc.date.accessioned2020-05-27T01:20:18Z-
dc.date.available2020-05-27T01:20:18Z-
dc.date.created2020-05-25-
dc.date.created2020-05-25-
dc.date.created2020-05-25-
dc.date.created2020-05-25-
dc.date.issued2020-05-
dc.identifier.citationCOMMUNICATIONS CHEMISTRY, v.3, no.1-
dc.identifier.issn2399-3669-
dc.identifier.urihttp://hdl.handle.net/10203/274316-
dc.description.abstractHypoxia-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.languageEnglish-
dc.publisherNATURE PUBLISHING GROUP-
dc.titleA human protein hydroxylase that accepts D-residues-
dc.typeArticle-
dc.identifier.wosid000531309700001-
dc.identifier.scopusid2-s2.0-85084154662-
dc.type.rimsART-
dc.citation.volume3-
dc.citation.issue1-
dc.citation.publicationnameCOMMUNICATIONS CHEMISTRY-
dc.identifier.doi10.1038/s42004-020-0290-5-
dc.contributor.localauthorHong, Sungwoo-
dc.contributor.nonIdAuthorChoi, Hwanho-
dc.contributor.nonIdAuthorHardy, Adam P.-
dc.contributor.nonIdAuthorLeissing, Thomas M.-
dc.contributor.nonIdAuthorChowdhury, Rasheduzzaman-
dc.contributor.nonIdAuthorNakashima, Yu-
dc.contributor.nonIdAuthorGe, Wei-
dc.contributor.nonIdAuthorMarkoulides, Marios-
dc.contributor.nonIdAuthorScotti, John S.-
dc.contributor.nonIdAuthorGerken, Philip A.-
dc.contributor.nonIdAuthorThorbjornsrud, Helen-
dc.contributor.nonIdAuthorLee, Joongoo-
dc.contributor.nonIdAuthorMcDonough, Michael A.-
dc.contributor.nonIdAuthorPark, Hwangseo-
dc.contributor.nonIdAuthorSchofield, Christopher J.-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordPlusANKYRIN REPEAT DOMAIN-
dc.subject.keywordPlusASPARAGINYL HYDROXYLASE-
dc.subject.keywordPlus2-OXOGLUTARATE-DEPENDENT OXYGENASES-
dc.subject.keywordPlusBETA-HYDROXYLATION-
dc.subject.keywordPlusHYPOXIA-
dc.subject.keywordPlusTRANSLATION-
dc.subject.keywordPlusDIOXYGENASE-
dc.subject.keywordPlusMECHANISMS-
dc.subject.keywordPlusSYNTHASE-
dc.subject.keywordPlusENZYMES-
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 6 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0