Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway

scientific article published on 26 May 2016

Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1007/S00775-016-1363-X
P932PMC publication ID4994471
P698PubMed publication ID27229511

P50authorJohn D. LipscombQ38327124
P2093author name stringElena G Kovaleva
Cory J Knoot
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Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implications for O2 activation by binuclear non-heme iron enzymesQ46323640
Reconstitution and characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidationQ46693381
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P433issue5-6
P407language of work or nameEnglishQ1860
P921main subjectchloramphenicolQ274515
P304page(s)589-603
P577publication date2016-05-26
P1433published inJournal of Biological Inorganic ChemistryQ3186899
P1476titleCrystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway
P478volume21

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cites work (P2860)
Q42328466A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase
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Q47930890CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates
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Q41581853X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a

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