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Structure and Function of Lactate Dehydrogenase from Hagfish

Faculty of Pharmaceutical Sciences, Toho University, Japan
Faculty of Science, Toho University, Japan
Author to whom correspondence should be addressed.
Mar. Drugs 2010, 8(3), 594-607;
Received: 8 January 2010 / Revised: 3 February 2010 / Accepted: 11 March 2010 / Published: 15 March 2010
(This article belongs to the Special Issue Enzymes from the Sea: Sources, Molecular Biology and Bioprocesses)
The lactate dehydrogenases (LDHs) in hagfish have been estimated to be the prototype of those in higher vertebrates. The effects of high hydrostatic pressure from 0.1 to 100 MPa on LDH activities from three hagfishes were examined. The LDH activities of Eptatretus burgeri, living at 45–60 m, were completely lost at 5 MPa. In contrast, LDH-A and -B in Eptatretus okinoseanus maintained 70% of their activities even at 100 MPa. These results show that the deeper the habitat, the higher the tolerance to pressure. To elucidate the molecular mechanisms for adaptation to high pressure, we compared the amino acid sequences and three-dimensional structures of LDHs in these hagfish. There were differences in six amino acids (6, 10, 20, 156, 269, and 341). These amino acidresidues are likely to contribute to the stability of the E. okinoseanus LDH under high-pressure conditions. The amino acids responsible for the pressure tolerance of hagfish are the same in both human and hagfish LDHs, and one substitution that occurred as an adaptation during evolution is coincident with that observed in a human disease. Mutation of these amino acids can cause anomalies that may be implicated in the development of human diseases. View Full-Text
Keywords: hagfish; lactate dehydrogenase; high-pressure adaptation; evolutionary medicine hagfish; lactate dehydrogenase; high-pressure adaptation; evolutionary medicine
MDPI and ACS Style

Nishiguchi, Y.; Ito, N.; Okada, M. Structure and Function of Lactate Dehydrogenase from Hagfish. Mar. Drugs 2010, 8, 594-607.

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