Abstract
Publisher Summary This chapter focuses on Histidine Ammonia-Lyase ( Pseudomonas ). Histidine ammonia-lyase from Pseudomonas is found to exist as a mixture of enzymatically active polymeric species held together by disulfide cross links. Each of the isolated monomeric and polymeric species is active without added thiols. Treatment with thiols, however, results in a 5- to 7-fold increase in activity associated with the liberation of 4 SH groups per monomer, titratable by the Ellman reagent. The enzyme is inhibited by sodium borohydride. After reduction of the enzyme with sodium borotritide, tritium-labeled alanine is found in the acid hydrolyzate, indicating that the enzyme contains dehydroalanine; under appropriate conditions L -histidine protects against inactivation, suggesting that dehydroalanine is at the active site of the enzyme.
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