| Autor: |
Bryant FO; Department of Biochemistry, University of Georgia, Athens 30602. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of enzyme inhibition [J Enzyme Inhib] 1991; Vol. 5 (3), pp. 235-48. |
| DOI: |
10.3109/14756369109080062 |
| Abstrakt: |
The L(+)-lactate dehydrogenase from Thermoanaerobacter ethanolicus wt was purified to a final specific activity of 598 mumol pyruvate reduced per min per mg of protein. The specific activity of the pure enzyme with L(+)-lactate was 0.79 units per mg of protein. The M(r) of the native enzyme was 134,000 containing a single subunit type of M(r) 33,500 indicating an apparent tetrameric structure. The L(+)-lactate dehydrogenase was activated by fructose 1,6-bisphosphate in a cooperative manner affecting Vmax and Km values. The activity of the enzyme was also effected by pH, pyruvate and NADH. The Km for NADH at pH 6.0 was 0.05 mM and the Vmax for pyruvate reduction at pH 6.0 was 1082 units per mg in the presence of 1 mM fructose 1,6-bisphosphate. The enzyme was inhibited by NADPH, displaying an uncompetitive pattern. This pattern indicated that NADPH was a negative modifier of the enzyme. The role of L(+)-lactate dehydrogenase in controlling the end products of fermentation is discussed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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