Publication: Characterization of cobalamin-dependent methionine synthase purified from the human malarial parasite, Plasmodium falciparum
Issued Date
1989-07-01
Resource Type
ISSN
14321955
00443255
00443255
Other identifier(s)
2-s2.0-0024372119
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Parasitology Research. Vol.75, No.7 (1989), 512-517
Suggested Citation
Jerapan Krungkrai, H. Kyle Webster, Yongyuth Yuthavong Characterization of cobalamin-dependent methionine synthase purified from the human malarial parasite, Plasmodium falciparum. Parasitology Research. Vol.75, No.7 (1989), 512-517. doi:10.1007/BF00931158 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/15755
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Title
Characterization of cobalamin-dependent methionine synthase purified from the human malarial parasite, Plasmodium falciparum
Abstract
Methionine synthase, which catalyzes the reaction, 5-methyltetrahydrofolate (5-CH 3 -H 4 PteGlu)+homocysteine→methionine+tetrahydrofolate, was detected and partially purified from the human malarial parasite, Plasmodium falciparum (K 1 isolate). Partial purification was achieved using high-performance size-exclusion and anion-exchange chromatography. The apparent relative molecular weight of the enzyme was estimated as 105000 daltons, and the apparent K m for 5-CH 3 -H 4 PteGlu was 24.2 μM. The enzyme was dependent on adenosylcobalamin or methylcobalamin but not on cobalamin, cyanocobalamin, or hydroxocobalamin in either the absence or presence of S-adenosylmethionine. Preincubation with nitrous oxide markedly inhibited the enzyme. Methionine synthase in P. falciparum may play a role in the supply of methionine and in folate salvage using exogenous 5-CH 3 -H 4 PteGlu for tetrahydrofolate metabolism. © 1989 Springer-Verlag.