A NOVEL GLUCOSE-6-PHOSPHATE-DEHYDROGENASE IN PLASMODIUM-FALCIPARUM - CDNA AND PRIMARY-PROTEIN STRUCTURE

被引：11

作者：

SHAHABUDDIN, M ^{[1
]}

RAWLINGS, DJ ^{[1
]}

KASLOW, DC ^{[1
]}

机构：

[1] NIAID,MOLEC VACCINE SECT,MALARIA RES LAB,BETHESDA,MD 20892

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1219卷 / 01期

关键词：

MALARIA; CLONING; HEXOSE MONOPHOSPHATE SHUNT; POLYMERASE CHAIN REACTION;

D O I：

10.1016/0167-4781(94)90269-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of the parasite-encoded G6PD (PfG6PD) may provide clues about the relative protection against malaria in humans with glucose-6-phosphate dehydrogenase (G6PD) deficiency. We have cloned Pfg6pd cDNA encoding a predicted 856 amino acid residues polypeptide with a calculated molecular mass of > 94 kDa. The predicted amino acid sequence is highly homologous to G6PD from other organisms. Pfg6pd maps as a single or low copy number gene to chromosome 14. The unusually large N-terminus and the distance between the NADP-binding site and G6PD-binding site is novel for the parasite G6PD. The differences between parasite and human G6PD proteins could potentially be exploited for designing new chemotherapeutic agents.

引用

页码：191 / 194

页数：4

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