{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T08:20:54Z","timestamp":1758874854533},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2001,12,25]],"date-time":"2001-12-25T00:00:00Z","timestamp":1009238400000},"content-version":"vor","delay-in-days":693,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2000,2]]},"abstract":"<jats:p>A single form of serine hydroxymethyltransferase (SHMT) was detected in epimastigotes of <jats:italic>Trypanosoma cruzi<\/jats:italic>, in contrast to the three isoforms of the enzyme characterized from another trypanosomatid, <jats:italic>Crithidia fasciculata<\/jats:italic>[Capelluto D.G.S., Hellman U., Cazzulo J.J. &amp; Cannata J.J.B. (1999) <jats:italic>Mol. Biochem. Parasitol.<\/jats:italic><jats:bold>98<\/jats:bold>, 187\u2013201]. The <jats:italic>T.\u2003cruzi<\/jats:italic> SHMT was found to be highly unstable in crude extracts. In the presence of the cysteine proteinase inhibitors <jats:italic>N<\/jats:italic>\u2010\u03b1\u2010<jats:italic>p<\/jats:italic>\u2010tosyl\u2010<jats:sc>l<\/jats:sc>\u2010lysine chloromethyl ketone and <jats:sc>l<\/jats:sc><jats:italic>trans<\/jats:italic>\u20103\u2010carboxyoxiran\u20102\u2010carbonyl\u2010<jats:sc>l<\/jats:sc>\u2010leucylagmatine, however, the enzyme could be purified to homogeneity. Digitonin treatment of intact cells suggested that the enzyme is cytosolic. <jats:italic>T.\u2003cruzi<\/jats:italic> SHMT presents a monomeric structure shown by the apparent molecular masses of 69\u2003kDa (native) and 55\u2003kDa (subunit) determined by Sephadex G\u2010200 gel filtration and SDS\/PAGE, respectively. This is in contrast to the tetrameric SHMTs described in <jats:italic>C.\u2003fasciculata<\/jats:italic> and other eukaryotes. The enzyme was pyridoxal phosphate\u2010dependent after <jats:sc>l<\/jats:sc>\u2010cysteine and hydroxylamine treatments and it was strongly inhibited by the substrate analog folate, which was competitive towards tetrahydrofolate and noncompetitive towards <jats:sc>l<\/jats:sc>\u2010serine. Partial sequencing of tryptic internal peptides of the enzyme indicate considerable similarity with other SHMTs, particularly from those of plant origin.<\/jats:p>","DOI":"10.1046\/j.1432-1327.2000.01047.x","type":"journal-article","created":{"date-parts":[[2003,3,11]],"date-time":"2003-03-11T18:00:40Z","timestamp":1047405640000},"page":"712-719","source":"Crossref","is-referenced-by-count":22,"title":["Purification and some properties of serine hydroxymethyltransferase from <i>Trypanosoma cruzi<\/i>"],"prefix":"10.1111","volume":"267","author":[{"given":"Daniel G. 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