The Proteases of Plasmodium: A Cathepsin D-like Enzyme from Plasmodium Lophurae

Sherman, I.W.; Tanigoshi, Linda

doi:10.1016/b978-0-08-026381-6.50016-4

Cited by 17 publications

(16 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A notable differencc between the two enzymes is the lowcr K,,, value of parasite GR for NADPH. The high affinity of the plasmodia1 enzyme for NADPH may bc advantageous in metabolic situations where the reducing cofactor becomes limiting (Sherman, 1979).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Glutathione Reductase and Glutamate Dehydrogenase of Plasmodium Falciparum, The Causative Agent of Tropical Malaria

Krauth‐Siegel

Müller

Lottspeich

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

The use of glutathione reductase inhibitors in chemotherapy is the raison d'&tre for this study. Two enzymes were purified to homogeneity from the intraerythrocytic malarial parasite Plasmodium falciparum : glutathione disulfide reductase, an antioxidative enzyme, which appears to play an essential role for parasite growth and differentiation, and glutamate dehydrogenase, an enzyme not occurring in the host erythrocyte. The two proteins were copurified and separated by gel electrophoresis with yields of approximately 20%. Malarial glutathione reductase, a homodimer of 110 kDa with a pH optimum of 6.8 and a high preference for NADPH over NADH, was shown to contain FAD as its prosthetic group. The N-terminal sequence, VYDLIVIGGGSGGMA, which can be aligned with residues 20-34 of human glutathione reductase, represents the first /j strand and the diphosphate-fixing helix of the FAD domain. Glutamate dehydrogenase was confirmed as a hexamer with blocked N-termini; it is an enzyme that is highly specific for NADP and NADPH. The copurification of the proteins and the potential of I? ,fulcipurunz glutathione reductase as a drug target are discussed.

show abstract

Section: Resultsmentioning

confidence: 99%

“…This enzyme, which connects nitrogen metabolism with the redox metabolism of the parasite (Walter et al, 1974;Sherman, 1979;Ling et al, 1986), is assumed to be the ma,jor source ol' the NADPH required for the reduction of glutathione disulfide (GSSG) by glutathione reduclase (Vander Jagt et al, 1989).…”

Section: -Oxoglutaratementioning

confidence: 99%

Glutathione Reductase and Glutamate Dehydrogenase of Plasmodium Falciparum, The Causative Agent of Tropical Malaria

Krauth‐Siegel

Müller

Lottspeich

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…The parasite can only synthesize pyrimidines de novo from HCO 3 -, ATP, glutamine, aspartate, and 5-phosphoribosyl-1-pyrophosphate [43][44][45][46][47][48][49][50][51][52][53] . These unique properties on both purine and pyrimidine requirement of the parasite are key differences from the human host, in which both functional de novo and salvage pathways of the purine and pyrimidine synthesis exists [46,48,[54][55][56][57][58].…”

Section: Basic Life Cycle Genomics and Biochemistry Of Human Malariamentioning

confidence: 99%

Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential

Krungkrai¹,

Krungkrai²

2011

Asian Pacific Journal of Tropical Biomedicine

View full text Add to dashboard Cite

“…Glutamate dehydrogenase (EC 1.4.1.4) has been demonstrated in several species of malarial parasites (Sherman, 1979). The predominant reaction is the oxidation of glutamate to a-ketoglutarate.…”

Section: Introductionmentioning

confidence: 99%

“…The asexual stages of malaria parasites can synthesize glutamate de novo by fixation of CO 2 (Sherman, 1979). Although human erythrocytes infected with P. falciparum remain relatively impermeable to glutamate, there is a large selective increase in permeability for glutamine (Elford, Haynes, Chulay & Wilson, 1985) which can be deaminated to glutamate.…”

Section: Introductionmentioning

confidence: 99%

Antibodies to the glutamate dehydrogenase ofPlasmodium falciparum

et al. 1986

View full text Add to dashboard Cite

SUMMARYPolyclonal antisera raised against Plasmodium, knowlesi reacted with (1) NADP-specific glutamate dehydrogenase (GLDH) of P. knowlesi, (2) GLDH of P. falciparum and (3) GLDH of Proteus spp. The antisera did not react with NAD(P) GLDH from bovine liver. Polyclonal antisera raised against the GLDH of Proteus spp. cross-reacted with GLDH from P. falciparum. Monoclonal antibodies (McAbs) obtained from mice immunized with Proteus GLDH were either specific for the bacterial enzyme or cross-reacted with P. falciparum GLDH. The selected McAbs did not react with GLDH from P. knowlesi, P. chabaudi or P. berghei. The GLDH of P'. falciparum was shown to be a cytosolic protein (by FAT) with a subunit molecular weight of approximately 49000 Da (by immunoprecipitation) having a predominantly hexameric form (by sucrose density gradient). Implications of the conserved sequences of GLDHs and other enzymes are discussed.

show abstract

The Proteases of Plasmodium: A Cathepsin D-like Enzyme from Plasmodium Lophurae

Cited by 17 publications

References 27 publications

Glutathione Reductase and Glutamate Dehydrogenase of Plasmodium Falciparum, The Causative Agent of Tropical Malaria

Glutathione Reductase and Glutamate Dehydrogenase of Plasmodium Falciparum, The Causative Agent of Tropical Malaria

Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential

Antibodies to the glutamate dehydrogenase ofPlasmodium falciparum

Contact Info

Product

Resources

About