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Microsomal oxygenases involved in ergoline alkaloid biosynthesis of various Claviceps strains
Author(s) -
Maier Walter,
Schumann Brigitte,
Gröger Detlef
Publication year - 1988
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620280111
Subject(s) - monooxygenase , oxygenase , biochemistry , enzyme , cytochrome , hydroxylation , microsome , cytochrome p450 , chemistry , stereochemistry
The conversions of agroclavine to elymoclavine and elymoclavine to paspalic acid/lysergic acid are catalyzed by microsomal preparations from various Claviceps strains. The enzymes designated as agroclavine 17‐monooxygenase and elymoclavine 17‐monooxygenase respectively are dependent on NADPH and molecular oxygen. NADH enhances enzyme activity observed in the presence of NADPH. Transhydrogenase activity in the presence of NADH and NADP + which is dependent on ATP was found. Carbon monoxide, as it was shown by K IM et al. (1981, 1983) and cytochrome c inhibit hydroxylation, whereas NACN did not affect the reactions. This and other properties suggest that both clavine specific enzymes are cytochrome P‐450 dependent monooxygenases. Lysergol was not converted by elymoclavine 17‐hydroxylase. Feedback inhibition of agroclavine 17‐monooxygenase by elymoclavine was demonstrated under in vitro conditions.