Regulation of lactate dehydrogenase activity in Rothia dentocariosa by fructose 1,6-diphosphate and adenosine 5'-triphosphate.
AUTOR(ES)
Eisenberg, R J
RESUMO
The L-(+)-lactate dehydrogenase from Rothia dentocariosa strain 17931 is activated by fructose 1,6-diphosphate and inhibited by adenosine 5'-triphosphate. The enzyme has a molecular weight of 120,000. In these respects, it resembles the lactate dehydrogenase of Actinomyces viscosus.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=233162Documentos Relacionados
- Inhibition of glucose 6-phosphate dehydrogenase by adenosine 5'-triphosphate.
- Purification and Properties of a Fructose-1,6-Diphosphate-Activated Lactate Dehydrogenase from Streptococcus faecalis
- Chloroplast and Cytoplasmic Enzymes: IV. Pea Leaf Fructose 1,6-Diphosphate Aldolases 12
- Fructose-1,6-Diphosphate-Dependent Lactate Dehydrogenase from a Cariogenic Streptococcus: Purification and Regulatory Properties
- Properties of Fructose 1,6-Diphosphate Aldolases from Spores and Vegetative Cells of Bacillus cereus1
