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Tryptophanase: structure, catalytic activities, and mechanism of action.
- E. Snell
- ChemistryAdvances in enzymology and related areas of…
- 22 November 2006
Pyridoxal phosphokinases. I. Assay, distribution, I. Assay, distribution, purification, and properties.
Purification and properties of a pyridoxal 5'-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15.
D-serine dehydratase from Escherichia coli. II. Analytical studies and subunit structure.
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.
PROPERTIES OF CRYSTALLINE TRYPTOPHANASE.
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.
- T. Gallagher, E. Snell, M. Hackert
- Chemistry, BiologyThe Journal of biological chemistry
- 25 July 1989
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.