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687 related items for PubMed ID: 14636074
1. Steady-state kinetics and tryptophan fluorescence properties of halohydrin dehalogenase from Agrobacterium radiobacter. Roles of W139 and W249 in the active site and halide-induced conformational change. Tang L, van Merode AE, Lutje Spelberg JH, Fraaije MW, Janssen DB. Biochemistry; 2003 Dec 02; 42(47):14057-65. PubMed ID: 14636074 [Abstract] [Full Text] [Related]
2. Improved catalytic properties of halohydrin dehalogenase by modification of the halide-binding site. Tang L, Torres Pazmiño DE, Fraaije MW, de Jong RM, Dijkstra BW, Janssen DB. Biochemistry; 2005 May 03; 44(17):6609-18. PubMed ID: 15850394 [Abstract] [Full Text] [Related]
3. Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from Agrobacterium radiobacter. Tang L, Lutje Spelberg JH, Fraaije MW, Janssen DB. Biochemistry; 2003 May 13; 42(18):5378-86. PubMed ID: 12731879 [Abstract] [Full Text] [Related]
4. Tryptophan fluorescence of the lux-specific Vibrio harveyi acyl-ACP thioesterase and its tryptophan mutants: structural properties and ligand-induced conformational change. Li J, Szittner R, Meighen EA. Biochemistry; 1998 Nov 17; 37(46):16130-8. PubMed ID: 9819205 [Abstract] [Full Text] [Related]
5. Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site. Krooshof GH, Ridder IS, Tepper AW, Vos GJ, Rozeboom HJ, Kalk KH, Dijkstra BW, Janssen DB. Biochemistry; 1998 Oct 27; 37(43):15013-23. PubMed ID: 9790663 [Abstract] [Full Text] [Related]
6. Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range. Schanstra JP, Ridder IS, Heimeriks GJ, Rink R, Poelarends GJ, Kalk KH, Dijkstra BW, Janssen DB. Biochemistry; 1996 Oct 08; 35(40):13186-95. PubMed ID: 8855957 [Abstract] [Full Text] [Related]
7. The effect of a unique halide-stabilizing residue on the catalytic properties of haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58. Hasan K, Gora A, Brezovsky J, Chaloupkova R, Moskalikova H, Fortova A, Nagata Y, Damborsky J, Prokop Z. FEBS J; 2013 Jul 08; 280(13):3149-59. PubMed ID: 23490078 [Abstract] [Full Text] [Related]
8. Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Castro C, Gratson AA, Evans JC, Jiracek J, Collinsová M, Ludwig ML, Garrow TA. Biochemistry; 2004 May 11; 43(18):5341-51. PubMed ID: 15122900 [Abstract] [Full Text] [Related]
9. Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter. Elbaz Y, Tayer N, Steinfels E, Steiner-Mordoch S, Schuldiner S. Biochemistry; 2005 May 17; 44(19):7369-77. PubMed ID: 15882076 [Abstract] [Full Text] [Related]
10. Photophysics of tryptophan fluorescence: link with the catalytic strategy of the citrate synthase from Thermoplasma acidophilum. Kurz LC, Fite B, Jean J, Park J, Erpelding T, Callis P. Biochemistry; 2005 Feb 08; 44(5):1394-413. PubMed ID: 15683225 [Abstract] [Full Text] [Related]
11. A fluorescence study of single tryptophan-containing mutants of enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent mannitol transport system. Dijkstra DS, Broos J, Lolkema JS, Enequist H, Minke W, Robillard GT. Biochemistry; 1996 May 28; 35(21):6628-34. PubMed ID: 8639611 [Abstract] [Full Text] [Related]
12. Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase. Zhang Y, Deshpande A, Xie Z, Natesh R, Acharya KR, Brew K. Glycobiology; 2004 Dec 28; 14(12):1295-302. PubMed ID: 15229192 [Abstract] [Full Text] [Related]
13. Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase. Li H, Jordan F. Biochemistry; 1999 Aug 03; 38(31):10004-12. PubMed ID: 10433707 [Abstract] [Full Text] [Related]
14. The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis. Azurmendi HF, Wang SC, Massiah MA, Poelarends GJ, Whitman CP, Mildvan AS. Biochemistry; 2004 Apr 13; 43(14):4082-91. PubMed ID: 15065850 [Abstract] [Full Text] [Related]
15. Identification of active site residues essential to 4-chlorobenzoyl-coenzyme A dehalogenase catalysis by chemical modification and site directed mutagenesis. Yang G, Liu RQ, Taylor KL, Xiang H, Price J, Dunaway-Mariano D. Biochemistry; 1996 Aug 20; 35(33):10879-85. PubMed ID: 8718880 [Abstract] [Full Text] [Related]
16. Activation of horse liver alcohol dehydrogenase upon substitution of tryptophan 314 at the dimer interface. Strasser F, Dey J, Eftink MR, Plapp BV. Arch Biochem Biophys; 1998 Oct 15; 358(2):369-76. PubMed ID: 9784252 [Abstract] [Full Text] [Related]
17. Repositioning the catalytic triad aspartic acid of haloalkane dehalogenase: effects on stability, kinetics, and structure. Krooshof GH, Kwant EM, Damborský J, Koca J, Janssen DB. Biochemistry; 1997 Aug 05; 36(31):9571-80. PubMed ID: 9236003 [Abstract] [Full Text] [Related]
18. Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway. Strambini GB, Cioni P, Cook PF. Biochemistry; 1996 Jun 25; 35(25):8392-400. PubMed ID: 8679597 [Abstract] [Full Text] [Related]
19. Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase. Zhang Z, Ostanin K, Van Etten RL. Acta Biochim Pol; 1997 Jun 25; 44(4):659-72. PubMed ID: 9584846 [Abstract] [Full Text] [Related]
20. Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Shao X, Matthews CR. Biochemistry; 1998 May 26; 37(21):7850-8. PubMed ID: 9601046 [Abstract] [Full Text] [Related] Page: [Next] [New Search]