Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Biotechnology Letters

Volumn 23, Issue 5, 2001, Pages 395-399

  Gül Karagüler, Nevin ^a,b   Sessions, Richard B ^b   Holbrook, J John ^b  

^a ISTANBUL TECHNICAL UNIVERSITY   (Turkey)

^b SCHOOL OF MEDICAL SCIENCES   (United Kingdom)

Author keywords

Lactate dehydrogenase; Site directed mutagenesis; Substrate inhibition

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; LACTATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BACILLUS STEAROTHERMOPHILUS; NONHUMAN; SITE DIRECTED MUTAGENESIS;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0035120153     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005687723905     Document Type: Article

References (10)

1. Cloning, expression and complete nuclcotide sequence of the Bacillus stearothermophilus
2. The molecular pathway by which fructose 1,6 bisphosphate induces the assembly of bacterial lactate dehydrogenase
3. Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus
4. Enzyme kinetics
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. Lactate dehydrogenase