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Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor urb597: Discovery of a deacylating water molecule and insight into enzyme inactivation

Academic Article
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Overview

authors

  • Mileni, M.
  • Kamtekar, S.
  • Wood, D. C.
  • Benson, T. E.
  • Cravatt, Benjamin
  • Stevens, Raymond

publication date

  • July 2010

journal

  • Journal of Molecular Biology  Journal

subject areas

  • Amidohydrolases
  • Benzamides
  • Carbamates
  • Catalytic Domain
  • Crystallography, X-Ray
  • Enzyme Inhibitors
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Tertiary
  • Water
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Research

keywords

  • URB597
  • catalytic mechanism
  • crystal structure
  • deacylating water
  • fatty acid amide hydrolase (FAAH)
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Identity

PubMed Central ID

  • PMC3014312

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2010.05.034

PubMed ID

  • 20493882
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Additional Document Info

start page

  • 743

end page

  • 754

volume

  • 400

issue

  • 4

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