Hassan H F, Coombs G H
Comp Biochem Physiol B. 1985;82(4):773-9. doi: 10.1016/0305-0491(85)90524-3.
Amastigotes and cultured promastigotes of Leishmania mexicana mexicana and L. m. amazonensis, cultured promastigotes of L. donovani and L. tarentolae, and the culture forms of Crithidia fasciculata, Herpetomonas muscarum muscarum and H. m. ingenoplastis all possessed four phosphoribosyltransferase (PRTase) activities: adenine PRTase, hypoxanthine PRTase, guanine PRTase and xanthine PRTase. The enzymes of L. m. mexicana required divalent cations for activity; Mn2+ or Co2+ produced maximal activity in most cases. Hypoxanthine PRTase, guanine PRTase and xanthine PRTase from all organisms were sedimentable in part, suggesting that they may occur within glycosomes. The enzymes of L. m. mexicana cultured promastigotes were inhibited by a range of purine analogues.
墨西哥利什曼原虫墨西哥亚种和亚马逊利什曼原虫的无鞭毛体及培养前鞭毛体、杜氏利什曼原虫和塔氏利什曼原虫的培养前鞭毛体，以及脆双核阿米巴、家蝇赫氏锥虫原虫型和家蝇赫氏锥虫无鞭毛体的培养形式均具有四种磷酸核糖基转移酶（PRTase）活性：腺嘌呤PRTase、次黄嘌呤PRTase、鸟嘌呤PRTase和黄嘌呤PRTase。墨西哥利什曼原虫墨西哥亚种的酶活性需要二价阳离子；在大多数情况下，Mn2+或Co2+可产生最大活性。所有生物体的次黄嘌呤PRTase、鸟嘌呤PRTase和黄嘌呤PRTase部分可沉降，这表明它们可能存在于糖体中。墨西哥利什曼原虫墨西哥亚种培养前鞭毛体的酶受到一系列嘌呤类似物的抑制。
