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Substrate Mimicry in an Activity-Based Probe That Targets the Nitrilase Family of Enzymes

Authors

  • Katherine T. Barglow,

    1. The Skaggs Institute for Chemical Biology and Departments of Cell Biology and Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-784-8023
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  • Benjamin F. Cravatt Prof.

    1. The Skaggs Institute for Chemical Biology and Departments of Cell Biology and Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-784-8023
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  • This research was supported by the NIH (CA087660), the Howard Hughes Medical Institute (predoctoral fellowship to K.T.B.), and the Skaggs Institute for Chemical Biology. We thank M. Patricelli (Activx Biosciences) for assistance with the identification of probe sites of labeling for nitrilase enzymes and the members of the Cravatt lab for helpful discussions and critical reading of the manuscript.

Abstract

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Drauf und dran: Ein Satz aktivitätsbasierter Proteomiksonden mit einem Dipeptid-α-Chloracetamid-Gerüst, das die Nitrilase-Enzymfamilie als Ziel hat, wird beschrieben. Ein Mitglied der Nitrilaseklasse, Ureidopropionase-β, reagiert selektiv mit einer speziellen Sonde, die das endogene Enzymsubstrat N-Carbamoyl-β-alanin nachahmt.

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