title: Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.
abstract: Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.
authors.affiliation: Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, 383 Yu Hang Tang Road, Hangzhou 310058, China.
authors.forename: Liuqing
authors.initials: L
authors.lastname: Yang
authors.forename: Marco
authors.initials: M
authors.lastname: Hill
authors.forename: Meitian
authors.initials: M
authors.lastname: Wang
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.forename: Joachim
authors.initials: J
authors.lastname: Stöckigt
mesh_terms: D019943:Amino Acid Substitution; D055162:Biocatalysis; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D050505:Mutant Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary; D046948:Secologanin Tryptamine Alkaloids / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D050505:Mutant Proteins; D046948:Secologanin Tryptamine Alkaloids; D002265:Carboxylic Ester Hydrolases; C463439:polyneuridine aldehyde esterase