Leartsakulpanich Ubolsree, Kongkasuriyachai Darin, Imwong Mallika, Chotivanich Kesinee, Yuthavong Yongyuth
National Center for Genetic Engineering and Biotechnology, 113 Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand.
Parasitol Int. 2008 Jun;57(2):223-8. doi: 10.1016/j.parint.2007.11.001. Epub 2007 Nov 12.
Serine hydroxymethyltransferase (SHMT), which catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate, is one of the three enzymes in dTMP synthesis pathway that is highly active during cell division and has been proposed as a potential chemotherapeutic target in infectious diseases and cancer. This is the first study to describe nucleotide and amino acid sequences of SHMT from the malaria parasite Plasmodium vivax. Sequencing of 12 P. vivax isolates revealed limited polymorphisms in 3 noncoding regions. Its biological function is also reported.
丝氨酸羟甲基转移酶（SHMT）催化丝氨酸和四氢叶酸可逆转化为甘氨酸和亚甲基四氢叶酸，它是dTMP合成途径中的三种酶之一，在细胞分裂过程中具有高活性，并且已被提议作为传染病和癌症的潜在化疗靶点。这是第一项描述间日疟原虫丝氨酸羟甲基转移酶核苷酸和氨基酸序列的研究。对12个间日疟原虫分离株进行测序，结果显示3个非编码区存在有限的多态性。本文还报道了其生物学功能。
