• Publications
  • Influence
Tryptophanase: structure, catalytic activities, and mechanism of action.
  • E. Snell
  • Chemistry
    Advances in enzymology and related areas of…
  • 22 November 2006
Pyruvoyl-dependent enzymes.
D-serine dehydratase from Escherichia coli. II. Analytical studies and subunit structure.
  • W. Dowhan, E. Snell
  • Biology, Chemistry
    The Journal of biological chemistry
  • 25 September 1970
An improved procedure which permits large scale preparation of crystalline d-serine dehydratase from Escherichia coli is described, and reaction of two or more with DTNB inactivates the apoenzyme completely by preventing its reassociation with pyridoxal-P.
The enzymatic oxidation of pyridoxine and pyridoxamine phosphates.
  • H. Wada, E. Snell
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1 July 1961
Argenine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme.
Abstract The inducible arginine decarboxylase of Escherichia coli, a pyridoxal-P enzyme, has been purified to a specific activity of 410 µmoles of CO2 per min per mg. It can be crystallized from
Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.
The structure of the pyruvoyl-dependent histidine decarboxylase has been refined to 2.5 A resolution by the methods of x-ray crystallography from crystals grown at pH 4.8, where the enzyme is
Purification and properties of pyridoxal-5'-phosphate-dependent histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes
These decarboxylases, all from gram-negative organisms, differed greatly in subunit structure, biogenesis, and other properties from the pyruvoyl-dependent histidine decar boxylases fromgram-positive organisms described previously.