2.5.1.2	analysis	improvements in a spectrophotometric thiaminase I activity assay that measures the disappearance of 4-nitrothiophenol providing scalable sample processing protocols and a 96-well microtiter plate format. Organisms devoid of thiaminase I, based upon previous work, show no activity with this assay. In addition, activity is found in a variety of fishes and one fern species from which this enzyme has not previously been reported	-, 739509	
2.5.1.2	medicine	-	636845	
2.5.1.2	medicine	bacteria can infect organisms and produce thiaminase disease	-, 636845	
2.5.1.2	medicine	ferns that have thiaminase produce thiamine deficiency in rat, cattle and horse	636845	
2.5.1.2	medicine	modification of thiaminase with linear chain methox polyethylene glycol of 5 kDa eliminates cytotoxic activity in all cell lines tested. Both native thiaminase and 5k-PEGylated thiaminase efficiently depletes thiamine from cell culture medium, and both can use intracellular phosphorylated thiamine as substrates. Native enzyme more effectively depletes thiamine and thiamine diphosphate in RS4 leukemia cell cytosol, and native thiaminase depresses cellular respiration, whereas PEGylated thiaminase does not. Despite the lack of in vitro cytotoxicity, PEGylation markedly increases the in vivo toxicity of the enzyme. The half-life of native thiaminase is 1.5 h compared with 34.4 h for the 5k-PEGylated enzyme. Serum thiamine levels are depleted by both native and 5k-PEGylated enzyme. Despite superior pharmacokinetics, 5k-PEGylated thiaminase shows no antitumor effect against an RS4 leukemia xenograft, in contrast to native thiaminase	723037	
2.5.1.2	medicine	plant extracts that have thiaminase activity can be toxic to animals or humans	636855	
2.5.1.2	medicine	thiamine transporter THTR2 downregulation in breast tumors may present a nutritional vulnerability that can be exploited by thiaminase I enzyme therapy	711655	
2.5.1.2	nutrition	thiaminase can be used as an effective method for thiamine determination in food and fodder	-, 636857