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Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity.
PMID: 4981920 [PubMed - indexed for MEDLINE]
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Cited by 12 PubMed Central articles
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Crystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of Pseudomonas aeruginosa amidase.
Andrade J, Karmali A, Carrondo MA, Frazão C.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1; 63(Pt 3):214-6. Epub 2007 Feb 23.
[Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007]
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Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.
Novo C, Farnaud S, Tata R, Clemente A, Brown PR.
Biochem J. 2002 Aug 1; 365(Pt 3):731-8.
[Biochem J. 2002]
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Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme.
Farnaud S, Tata R, Sohi MK, Wan T, Brown PR, Sutton BJ.
Biochem J. 1999 Jun 15; 340 ( Pt 3):711-4.
[Biochem J. 1999]
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