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Journal Abstract Search


245 related items for PubMed ID: 11955282

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  • 3. Pseudomonas aeruginosa aliphatic amidase is related to the nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism.
    Novo C, Tata R, Clemente A, Brown PR.
    FEBS Lett; 1995 Jul 03; 367(3):275-9. PubMed ID: 7607322
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  • 4. Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: identification of catalytic residues.
    Amara AA, Rehm BH.
    Biochem J; 2003 Sep 01; 374(Pt 2):413-21. PubMed ID: 12924980
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  • 7. Crystal structure analysis of a bacterial aryl acylamidase belonging to the amidase signature enzyme family.
    Lee S, Park EH, Ko HJ, Bang WG, Kim HY, Kim KH, Choi IG.
    Biochem Biophys Res Commun; 2015 Nov 13; 467(2):268-74. PubMed ID: 26454172
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  • 8. Catalysis in the nitrilase superfamily.
    Brenner C.
    Curr Opin Struct Biol; 2002 Dec 13; 12(6):775-82. PubMed ID: 12504683
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  • 10. Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation.
    Katiyar S, Suzuki T, Balgobin BJ, Lennarz WJ.
    J Biol Chem; 2002 Apr 12; 277(15):12953-9. PubMed ID: 11812789
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  • 11. Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway.
    Kim MK, Oh SJ, Lee BG, Song HK.
    Proc Natl Acad Sci U S A; 2016 Nov 01; 113(44):12438-12443. PubMed ID: 27791147
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  • 12. Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability.
    Karmali A, Pacheco R, Tata R, Brown P.
    Mol Biotechnol; 2001 Mar 01; 17(3):201-12. PubMed ID: 11434308
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  • 13. Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state.
    Andrade J, Karmali A, Carrondo MA, Frazão C.
    J Biol Chem; 2007 Jul 06; 282(27):19598-605. PubMed ID: 17442671
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  • 14. Crystal structure of the CN-hydrolase SA0302 from the pathogenic bacterium Staphylococcus aureus belonging to the Nit and NitFhit Branch of the nitrilase superfamily.
    Gordon RD, Qiu W, Romanov V, Lam K, Soloveychik M, Benetteraj D, Battaile KP, Chirgadze YN, Pai EF, Chirgadze NY.
    J Biomol Struct Dyn; 2013 Oct 06; 31(10):1057-65. PubMed ID: 23607706
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  • 16. An alternative mechanism for amidase signature enzymes.
    Labahn J, Neumann S, Büldt G, Kula MR, Granzin J.
    J Mol Biol; 2002 Oct 04; 322(5):1053-64. PubMed ID: 12367528
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  • 17. The signature amidase from Sulfolobus solfataricus belongs to the CX3C subgroup of enzymes cleaving both amides and nitriles. Ser195 and Cys145 are predicted to be the active site nucleophiles.
    Cilia E, Fabbri A, Uriani M, Scialdone GG, Ammendola S.
    FEBS J; 2005 Sep 04; 272(18):4716-24. PubMed ID: 16156792
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  • 18. Amino acid homologies between human biotinidase and bacterial aliphatic amidases: putative identification of the active site of biotinidase.
    Swango KL, Hymes J, Brown P, Wolf B.
    Mol Genet Metab; 2000 Feb 04; 69(2):111-5. PubMed ID: 10720437
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  • 19. Using directed evolution to probe the substrate specificity of mandelamide hydrolase.
    Wang PF, Yep A, Kenyon GL, McLeish MJ.
    Protein Eng Des Sel; 2009 Feb 04; 22(2):103-10. PubMed ID: 19074156
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  • 20. 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)(Pt 3):711-4. PubMed ID: 10359655
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