Mutagenic exploration of the active site of lactate dehydrogenase from Plasmodium falciparum

Biotechnology Letters

Volumn 23, Issue 11, 2001, Pages 923-927

  Turgut Balik, Dilek ^a   Shoemark, Debbie K ^b   Sessions, Richard B ^b   Moreton, Kathleen M ^b   Holbrook, J John ^b  

^a FIRAT UNIVERSITY   (Turkey)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Anti malarials; Drug resistance; Enzyme; Malaria; Substrate specificity loop

Indexed keywords

LACTATE DEHYDROGENASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE DELETION; NONHUMAN; PLASMODIUM FALCIPARUM; SITE DIRECTED MUTAGENESIS;

PLASMODIUM FALCIPARUM; PROTOZOA;

EID: 0034963704     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010507904515     Document Type: Article

References (13)

1. On the effect on specificity of Thr246Gly mutation in L-lactate dehydrogenase of Bacillus stearothermophilus
2. The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial drug design
3. Design and synthesis of new enzymes based on the lactate dehydrogenase framework
4. Engineering surface loops of proteins - A preferred strategy for obtaining new enzyme function
5. Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change
6. A general method for relieving substrate inhibition in lactate dehydrogenases
7. Protein engineering tests of a homology model of Plasmodium falciparum lactate dehydrogenase
8. Cancer multidrug resistance
9. Malaria
10. Structural basis for altered activity of M and H isozyme forms of human lactate dehydrogenase
11. Over-production of lactate dehydrogenase from Plasmodium falciparum opens a route to new antimalarials
12. Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 Å resolution
13. Design of a specific phenyl-lactate dehydrogenase by peptide loop exchange on the Bacillus stearothermophilus lactate dehydrogenase framework