title: Design and synthesis of chromogenic thiopeptolide substrates as MetAPs active site probes.
abstract: Twenty one chromogenic thiopeptolide substrates were designed and synthesized as the active site probes and analyzed with each S1 site of mutant residues and enzymes of wild-type MetAP1s. The preliminary enzymatic experiments indicate that cysteine 70 or 202, at either Escherichia coli or human MetAP1, played a crucial role in the methionine hydrolysis.
authors.affiliation: Chinese National Center for Drug Screening, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 189 Guo Shou Jing Road, ZhangJiang Hi-Tech Park, Shanghai 201203, China.
authors.forename: Yong-Mei
authors.initials: YM
authors.lastname: Cui
authors.forename: Jing-Ya
authors.initials: JY
authors.lastname: Li
authors.forename: Ling-Ling
authors.initials: LL
authors.lastname: Chen
authors.forename: Jia
authors.initials: J
authors.lastname: Li
authors.forename: Qi-Zhuang
authors.initials: QZ
authors.lastname: Ye
authors.forename: Fa-Jun
authors.initials: FJ
authors.lastname: Nan
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002863:Chromogenic Compounds / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D003524:Cyclosporins / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D008715:Methionine / Q000378:metabolism*; D063208:Methionyl Aminopeptidases; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D017354:Point Mutation; D013438:Sulfhydryl Compounds / Q000032:analysis
chemical_list: D002863:Chromogenic Compounds; D003524:Cyclosporins; D009842:Oligopeptides; D013438:Sulfhydryl Compounds; D008715:Methionine; D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases