Thiaminases and Thiamin Antagonists

Thieiminase II catalyzes a simple hydrolysis, releasing thiazole and meth-oxypyrimidine, which has some antivitamin Bg antimetabolic activity. It is relatively rare and is restricted to a small number of microorganisms. 

In people whose thiamin intake is marginal, colonization of the gastrointestinal tract with thiaminolytic microorganisms may be a factor in the development of beriberi. The thiaminases present in raw fish can result in so-called Chastek paralysis of foxes and mink, as a result of destruction of thiamin, and may be important in parts of the world where much of the apparent thiamin intake is from fish that is eaten raw or fermented. The polyphenols and thiami-nase in bracken fern can cause thiamin deficiency (blind staggers) in horses, and tannic acid in tea and betel nut have been associated with human thiamin deficiency. 

There are two classes of thiaminase. Thiaminase I catalyzes a base exchange reaction between the thiazole moiety of thiamin and a variety of bases, commonly primary, secondary, or tertiary amines, but also nicotincimide and other pyridine derivatives, and sometimes proline tmd sulfhydryl compounds. Thiaminase I is relatively widespread in a veuiety of microorgcmisms, plcmts, cmd fish. In addition to depleting thiamin, the products of base exchange catedyzed by thiaminase I eire structured emedogs of the viteimin and may have antagonistic effects (Edwin and Jackman, 1970). Similarly, the neurotoxic effects of the antibiotic metronidazole, which is a thiazole, may be fi om its activity as a substrate for thieiminase I, forming thiamin antimetabolites (Alston emd Abeles, 1987). 

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