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Formyl migration product of chanoclavine‐I aldehyde in the presence of the old yellow enzyme FgaOx3 from Aspergillus fumigatus : a NMR structure elucidation
Author(s) -
Xie Xiulan,
Wallwey Christiane,
Matuschek Marco,
Steinbach Klaus,
Li ShuMing
Publication year - 2011
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.2796
Subject(s) - chemistry , aspergillus fumigatus , aldehyde , stereochemistry , enzyme , heteronuclear single quantum coherence spectroscopy , formamide , two dimensional nuclear magnetic resonance spectroscopy , carbon 13 nmr , biosynthesis , biochemistry , organic chemistry , catalysis , microbiology and biotechnology , biology
A previous study showed that together with the festuclavine synthase FgaFS, the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyzed the conversion of chanoclavine‐I aldehyde to festuclavine in the biosynthesis of ergot alkaloids. In the absence of FgaFS, a mixture containing two compounds with a ratio of 7:3 was detected in the enzyme assay of FgaOx3. NMR experiments including (DQF)‐COSY, HSQC, HMBC and NOESY identified their structures as E / Z isomers of N ‐methyl‐ N ‐[(5R,10R)‐10‐(2‐oxo‐propyl)‐2,4,5,10‐tetrahydrobenzo[cd]indol‐5‐yl]formamide and proved the migration of the formyl group at C‐8 in chanoclavine I‐aldehyde to N‐6 in the identified products. Copyright © 2011 John Wiley & Sons, Ltd.