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Items: 5

1.
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.
Carlos Novo, Sebastien Farnaud, Renée Tata, Alda Clemente, Paul R Brown
Biochem J. 2002 Aug 1; 365(Pt 3): 731–738. doi: 10.1042/BJ20011714
PMCID:
PMC1222709
SummaryPDF–331K
2.
Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme.
S Farnaud, R Tata, M K Sohi, T Wan, P R Brown, B J Sutton
Biochem J. 1999 Jun 15; 340(Pt 3): 711–714.
PMCID:
PMC1220302
SummaryPDF–127K
3.
Transcriptional analysis of the amidase operon from Pseudomonas aeruginosa.
S A Wilson, R E Drew
J Bacteriol. 1995 Jun; 177(11): 3052–3057. doi: 10.1128/jb.177.11.3052-3057.1995
PMCID:
PMC176992
SummaryPDF–306K
4.
Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50
Sandra Trott, Sibylle Bürger, Carsten Calaminus, Andreas Stolz
Appl Environ Microbiol. 2002 Jul; 68(7): 3279–3286. doi: 10.1128/AEM.68.7.3279-3286.2002
PMCID:
PMC126760
ArticlePDF–144K
5.
Characterization of Plant β-Ureidopropionase and Functional Overexpression in Escherichia coli
Terence A. Walsh, Susan B. Green, Ignacio M. Larrinua, Paul R. Schmitzer
Plant Physiol. 2001 Feb; 125(2): 1001–1011. doi: 10.1104/pp.125.2.1001
PMCID:
PMC64900
ArticlePDF–507K

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