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9. Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the mutation of Tyrosine 72 to phenylalanine, and its mechanistic consequences. Kulikova VV; Zakomirdina LN; Dementieva IS; Phillips RS; Gollnick PD; Demidkina TV; Faleev NG Biochim Biophys Acta; 2006 Apr; 1764(4):750-7. PubMed ID: 16455316 [TBL] [Abstract][Full Text] [Related]
10. The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation. Tsesin N; Kogan A; Gdalevsky GY; Himanen JP; Cohen-Luria R; Parola AH; Goldgur Y; Almog O Acta Crystallogr D Biol Crystallogr; 2007 Sep; 63(Pt 9):969-74. PubMed ID: 17704565 [TBL] [Abstract][Full Text] [Related]
11. Structure of Escherichia coli tryptophanase. Ku SY; Yip P; Howell PL Acta Crystallogr D Biol Crystallogr; 2006 Jul; 62(Pt 7):814-23. PubMed ID: 16790938 [TBL] [Abstract][Full Text] [Related]
12. Crystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris. Dementieva IS; Zakomirdina LN; Sinitzina NI; Antson AA; Wilson KS; Isupov MN; Lebedev AA; Harutyunyan EH J Mol Biol; 1994 Jan; 235(2):783-6. PubMed ID: 8289300 [TBL] [Abstract][Full Text] [Related]
13. Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli. Kawata Y; Tsujimoto N; Tani S; Mizobata T; Tokushige M Biochem Biophys Res Commun; 1990 Dec; 173(2):756-62. PubMed ID: 2260981 [TBL] [Abstract][Full Text] [Related]
14. Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents. Faleev NG; Dementieva IS; Zakomirdina LN; Gogoleva OI; Belikov VM Biochem Mol Biol Int; 1994 Aug; 34(1):209-16. PubMed ID: 7849621 [TBL] [Abstract][Full Text] [Related]
16. Characterization of the tryptophanase operon of Proteus vulgaris. Cloning, nucleotide sequence, amino acid homology, and in vitro synthesis of the leader peptide and regulatory analysis. Kamath AV; Yanofsky C J Biol Chem; 1992 Oct; 267(28):19978-85. PubMed ID: 1400314 [TBL] [Abstract][Full Text] [Related]
17. Replacement of lysine 269 by arginine in Escherichia coli tryptophan indole-lyase affects the formation and breakdown of quinonoid complexes. Phillips RS; Richter I; Gollnick P; Brzovic P; Dunn MF J Biol Chem; 1991 Oct; 266(28):18642-8. PubMed ID: 1917987 [TBL] [Abstract][Full Text] [Related]
18. Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase. Phillips RS; Holtermann G Biochemistry; 2005 Nov; 44(43):14289-97. PubMed ID: 16245945 [TBL] [Abstract][Full Text] [Related]
19. Effects of alpha-deuteration and of aza and thia analogs of L-tryptophan on formation of intermediates in the reaction of Escherichia coli tryptophan indole-lyase. Sloan MJ; Phillips RS Biochemistry; 1996 Dec; 35(50):16165-73. PubMed ID: 8973188 [TBL] [Abstract][Full Text] [Related]
20. Cleavage of Escherichia coli tryptophan indole-lyase by trypsin at Lys406 affects the transmission of conformational changes associated with monovalent cation activation. Phillips RS; Doshi KJ Eur J Biochem; 1998 Jul; 255(2):508-15. PubMed ID: 9716394 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]