Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli
- 1 December 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 173 (2), 756-762
- https://doi.org/10.1016/s0006-291x(05)80100-7
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Three-Dimensional Structures of Aspartate Aminotransferase from Escherichia coli and Its Mutant Enzyme at 2.5 Å ResolutionThe Journal of Biochemistry, 1990
- Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of aspartate aminotransferaseBiochemical and Biophysical Research Communications, 1990
- Role of cysteine residues in tryptophanase for monovalent cation-induced activationBiochimie, 1989
- Synthesis of l-tyrosine from phenol and catalysed by tyrosine phenol-lyaseEnzyme and Microbial Technology, 1989
- The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNANucleic Acids Research, 1985
- Fluorescence energy transfer in tryptophanaseBiochemical and Biophysical Research Communications, 1980
- Ozonization of the tryptophyl residue in tryptophanaseBiochemical and Biophysical Research Communications, 1979
- Direct spectrophotometric assay of tryptophanaseFEBS Letters, 1976
- Preparation and characterization of several new immobilized derivatives of pyridoxal 5′-phosphateBiochimica et Biophysica Acta (BBA) - General Subjects, 1974
- [54] Tryptophanase (Escherichia coli B)Published by Elsevier ,1970