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Journal Abstract Search


106 related items for PubMed ID: 21266781

  • 1. Identification of the catalytic residues of carboxylesterase from Arthrobacter globiformis by diisopropyl fluorophosphate-labeling and site-directed mutagenesis.
    Nishizawa M, Yabusaki Y, Kanaoka M.
    Biosci Biotechnol Biochem; 2011; 75(1):89-94. PubMed ID: 21266781
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  • 2. Stereoselective production of (+)-trans-chrysanthemic acid by a microbial esterase: cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli.
    Nishizawa M, Shimizu M, Ohkawa H, Kanaoka M.
    Appl Environ Microbiol; 1995 Sep; 61(9):3208-15. PubMed ID: 7574629
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  • 3. Tryptophan-216 is essential for the transglycosylation activity of endo-beta-N-acetylglucosaminidase A.
    Fujita K, Takegawa K.
    Biochem Biophys Res Commun; 2001 May 11; 283(3):680-6. PubMed ID: 11341779
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  • 4. Identification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling.
    Choi YH, Lee YN, Park YJ, Yoon SJ, Lee HB.
    BMB Rep; 2016 Jun 11; 49(6):349-54. PubMed ID: 27222124
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  • 5. Key amino acid associated with acephate detoxification by Cydia pomonella carboxylesterase based on molecular dynamics with alanine scanning and site-directed mutagenesis.
    Yang XQ, Liu JY, Li XC, Chen MH, Zhang YL.
    J Chem Inf Model; 2014 May 27; 54(5):1356-70. PubMed ID: 24749772
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  • 9. Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis.
    Ogata S, Misumi Y, Tsuji E, Takami N, Oda K, Ikehara Y.
    Biochemistry; 1992 Mar 10; 31(9):2582-7. PubMed ID: 1347701
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  • 10. Expression and characterization of the carboxyl esterase Rv3487c from Mycobacterium tuberculosis.
    Zhang M, Wang JD, Li ZF, Xie J, Yang YP, Zhong Y, Wang HH.
    Protein Expr Purif; 2005 Jul 10; 42(1):59-66. PubMed ID: 15939293
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  • 11. Site-directed mutagenesis establishes aspartic acids-227 and -342 as essential for enzyme activity in an isomalto-dextranase from Arthrobacter globiformis.
    Tochihara T, Sasaki K, Araki O, Morimoto N, Watanabe K, Hatada Y, Ito S, Ito H, Matsui H.
    Biotechnol Lett; 2004 Apr 10; 26(8):659-64. PubMed ID: 15200177
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  • 16. Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
    Harris JM, McIntosh EM, Muscat GE.
    J Mol Biol; 1999 Apr 30; 288(2):275-87. PubMed ID: 10329142
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  • 19. Role of the N-terminal domain of endoinulinase from Arthrobacter sp. S37 in regulation of enzyme catalysis.
    Kim KY, Rhee S, Kim SI.
    J Biochem; 2005 Jul 30; 138(1):27-33. PubMed ID: 16046445
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