Literature DB >> 4860552

Interactions between the subunits of the tryptophan synthetase of Escherichia coli. Optical properties of an intermediate bound to the alpha-2 beta-2 complex.

M E Goldberg, R L Baldwin.   

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Year:  1967        PMID： 4860552     DOI： 10.1021/bi00859a032

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  3 in total

Review 1.  Synthesis of optically active sulfur and selenium amino acids with microbial enzymes.

Authors:  H Tanaka; N Esaki; K Soda
Journal:  Appl Biochem Biotechnol       Date:  1985-02       Impact factor: 2.926

2.  Inhibition of tryptophan synthetase by indoleacrylic acid.

Authors:  W H Matchett
Journal:  J Bacteriol       Date:  1972-04       Impact factor: 3.490

3.  Protonation states of the tryptophan synthase internal aldimine active site from solid-state NMR spectroscopy: direct observation of the protonated Schiff base linkage to pyridoxal-5'-phosphate.

Authors:  Bethany G Caulkins; Baback Bastin; Chen Yang; Thomas J Neubauer; Robert P Young; Eduardo Hilario; Yu-ming M Huang; Chia-en A Chang; Li Fan; Michael F Dunn; Michael J Marsella; Leonard J Mueller
Journal:  J Am Chem Soc       Date:  2014-09-03       Impact factor: 15.419
  3 in total

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