Stereochemistry of sodium borohydride reduction of tryptophan synthase of Escherichia coli and its amino acid Schiff's bases.
Open Access
- 1 December 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (23) , 14203-14210
- https://doi.org/10.1016/s0021-9258(19)45366-0
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- An active proteolytic derivative of the .alpha. subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragmentsBiochemistry, 1979
- Mechanism of action of D-serine dehydratase. Identification of a transient intermediateBiochemistry, 1979
- Stereospecificity of sodium borohydride reduction of tyrosine decarboxylase from Streptococcus faecalis.Journal of Biological Chemistry, 1979
- Stereochemistry and mechanism of reactions catalyzed by tryptophan synthetase and its beta2 subunitJournal of Biological Chemistry, 1978
- Stereochemistry and mechanism of reactions catalyzed by tryptophanase Escherichia coliJournal of Biological Chemistry, 1978
- Tryptophan synthase of Escherichia coli. Removal of pyridoxal 5'-phosphate and separation of the alpha and beta2 subunits.Journal of Biological Chemistry, 1977
- A Kinetic Study of the Reaction Mechanism of Tryptophanase-catalyzed ReactionsJournal of Biological Chemistry, 1967
- DARSTELLUNG VON RADIOAKTIV MARKIERTEM PYRIDOXAL-5'-PHOSPHAT1966
- ENZYMATIC TRANSAMINATION OF PYRIDOXAMINE .1. WITH OXALOACETATE AND ALPHA-KETOGLUTARATE1962
- The Enzymatic Oxidation of Pyridoxine and Pyridoxamine PhosphatesJournal of Biological Chemistry, 1961