Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase

Ubolsree Leartsakulpanich; Darin Kongkasuriyachai; Mallika Imwong; Kesinee Chotivanich; Yongyuth Yuthavong

doi:10.1016/j.parint.2007.11.001

Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase

Ubolsree Leartsakulpanich
, Darin Kongkasuriyachai
, Mallika Imwong
, Kesinee Chotivanich
, Yongyuth Yuthavong

National Science and Technology Development Agency (NSTDA)

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	223-228
Number of pages	6
Journal	Parasitology International
Volume	57
Issue number	2
DOIs	https://doi.org/10.1016/j.parint.2007.11.001
Publication status	Published - Jun 2008

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Plasmodium vivax
Serine hydroxymethyltransferase
dTMP cycle

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10.1016/j.parint.2007.11.001

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title = "Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase",

abstract = "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.",

keywords = "Plasmodium vivax, Serine hydroxymethyltransferase, dTMP cycle",

author = "Ubolsree Leartsakulpanich and Darin Kongkasuriyachai and Mallika Imwong and Kesinee Chotivanich and Yongyuth Yuthavong",

year = "2008",

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T1 - Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase

AU - Leartsakulpanich, Ubolsree

AU - Kongkasuriyachai, Darin

AU - Imwong, Mallika

AU - Chotivanich, Kesinee

AU - Yuthavong, Yongyuth

PY - 2008/6

Y1 - 2008/6

N2 - 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.

AB - 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.

KW - Plasmodium vivax

KW - Serine hydroxymethyltransferase

KW - dTMP cycle

UR - https://www.scopus.com/pages/publications/40849089375

U2 - 10.1016/j.parint.2007.11.001

DO - 10.1016/j.parint.2007.11.001

M3 - Article

C2 - 18096429

AN - SCOPUS:40849089375

SN - 1383-5769

VL - 57

SP - 223

EP - 228

JO - Parasitology International

JF - Parasitology International

IS - 2

ER -

Cloning and characterization of Plasmodium vivax serine hydroxymethyltransferase

Abstract

UN SDGs

Keywords

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