Entry Name Class Ligases;BRITE hierarchy
Sysname S-adenosyl-L-methionine:anthranilate:L-phenylalanine ligase (cyclopeptine-forming)
Reaction(IUBMB) 2 ATP + S-adenosyl-L-methionine + anthranilate + L-phenylalanine = cyclopeptine + 2 AMP + 2 diphosphate + S-adenosyl-L-homocysteine [RN:
R10495 ]
Reaction(KEGG) Substrate Product Comment Cyclopeptine synthase is the key enzyme of benzodiazepine alkaloid biosynthesis in several fungi species. The enzyme is a non-ribosomal peptide synthase. It is also active with O-methyl-L-tyrosine forming 4'-methoxycyclopeptine.
History EC 6.3.2.40 created 2013
Orthology Genes Taxonomy Reference Authors Lerbs W, Luckner M.
Title Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium.
Journal Reference 2
Authors Gerlach, M, Schwelle, N., Lerbs, W. and Luckner, M.
Title Enzymatic synthesis of cyclopeptine intermediates in Penicillium cyclopium.
Journal Phytochemistry 24:1935-1939 (1985)
Reference Authors Ishikawa N, Tanaka H, Koyama F, Noguchi H, Wang CC, Hotta K, Watanabe K
Title Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alkaloids.
Journal Other DBs ExplorEnz - The Enzyme Database: 6.3.2.40
ExPASy - ENZYME nomenclature database: 6.3.2.40
