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B6db references: 241324

type Journal Article
authors Hacking, A. J.; Hassall, H.
title The purification and properties of L-histidine--2-oxoglutarate aminotransferase from Pseudomonas testosteroni
journal Biochem J
sel selected
ui 241324
year (1975)
volume 147
number 2
pages 327-34
keywords Chromatography, DEAE-Cellulose
abstract 1. Inducible L-histidine--2-oxoglutarate aminotransferase was purified some 170-fold from extracts of Pseudomonas testosteroni. 2. The preparation showed only one major component after electrophoresis on polyacrylamide gels, though additional minor bands were observed when samples concentrated on a DEAE-cellulose column were used. 3. The molecular weight of the enzyme was found to be approx. 70000 by chromatography on Sephadex G-200. 4. The purification scheme produced enzyme that was inactive in the absence of pyridoxal 5'-phosphate. 5. The equilibrium constant for the reaction L-histidine+2-oxoglutarate equilibrium imidazolylpyruvate+L-glutamate was 0.49. 6. The reaction mechanism was Ping Pong. 7. The enzyme was shown to have only low activity towards aromatic amino acids and was highly specific for 2- oxoglutarate.
last changed 2009/05/04 16:32

B6db references