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Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling.
Kasai, Shota; Konno, Sho; Ishikawa, Fumihiro; Kakeya, Hideaki.
Afiliação
  • Kasai S; Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
  • Konno S; Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
  • Ishikawa F; Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
  • Kakeya H; Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. fishika@pharm.kyoto-u.ac.jp scseigyo-hisyo@pharm.kyoto-u.ac.jp.
Chem Commun (Camb) ; 51(87): 15764-7, 2015 Nov 11.
Article em En | MEDLINE | ID: mdl-26365322
ABSTRACT
We describe competitive activity-based protein profiling (ABPP) to accelerate the functional prediction and assessment of adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) in proteomic environments. Using a library of sulfamoyloxy-linked aminoacyl-AMP analogs, the competitive ABPP technique offers a simple and rapid assay system for adenylating enzymes and provides insight into enzyme substrate candidates and enzyme active-site architecture.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Sintases Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2015 Tipo de documento: Article