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Lactate Dehydrogenase(LDH) is a large, two domain- protein which catalyzes the conversion of pyruvate to lactate under anaerobic conditions.<ref>DOI 10.1126/science.1160809</ref> This conversion is coupled with the reduction of NAD+ to form the electron carrying NADH. Muscular LDH is involved in the Cori Cycle where it transports newly synthesized lactate to the liver. Liver LDH converts the lactate back to pyruvate in order to provide the precursor for gluconeogenesis.<ref>DOI 10.1126/science.136.3520.962</ref>
Lactate Dehydrogenase(LDH) is a large, two domain- protein which catalyzes the conversion of pyruvate to lactate under anaerobic conditions.<ref>DOI 10.1126/science.1160809</ref> This conversion is coupled with the reduction of NAD+ to form the electron carrying NADH. Muscular LDH is involved in the Cori Cycle where it transports newly synthesized lactate to the liver. Liver LDH converts the lactate back to pyruvate in order to provide the precursor for gluconeogenesis.<ref>DOI 10.1126/science.136.3520.962</ref>
== Disease ==
== Disease ==
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Lactate dehydrogenase is found in its various isoenzyme forms throughout the body, including: brain, red blood cells, lungs, kidney, placenta, pancreas, muscle, and liver. It is kept at relatively low concentrations and is only utilized as a pathway under anaerobic conditions as it produces less ATP/glucose than oxidative phosphorylation. High levels of LDH are generally indicative of poor health. LDH translation is found to be overly expressed in pancreatic cancer and showed correlation with cell growth success rate. <ref>DOI 10.1126/science.1160809</ref><ref>10.1007/s13277-013-0679-1</ref>
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Lactate dehydrogenase is found in its various isoenzyme forms throughout the body, including: brain, red blood cells, lungs, kidney, placenta, pancreas, muscle, and liver. It is kept at relatively low concentrations and is only utilized as a pathway under anaerobic conditions as it produces less ATP/glucose than oxidative phosphorylation. High levels of LDH are generally indicative of poor health. LDH translation is found to be overly expressed in pancreatic cancer and showed correlation with cell growth success rate. <ref>DOI 10.1126/science.1160809</ref> <ref>10.1007/s13277-013-0679-1</ref>
Increased LDH levels are also associated with conditions such as Rhabdomyolysis which is characterized by the breakdown of skeletal muscle. This is due in part to LDH in red blood cells being released through hemolysis.
Increased LDH levels are also associated with conditions such as Rhabdomyolysis which is characterized by the breakdown of skeletal muscle. This is due in part to LDH in red blood cells being released through hemolysis.
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</StructureSection>
</StructureSection>
== References ==
== References ==
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<ref>DOI 10.3390/molecules22122217</ref>
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<ref>DOI 10.1126/science.1160809</ref>
<ref>DOI 10.1126/science.1160809</ref>
<ref>10.1007/s13277-013-0679-1</ref>
<ref>10.1007/s13277-013-0679-1</ref>

Revision as of 03:13, 22 April 2018

Crystal Structure of Lactate Dehydrogenase A in complex with the inhibitor, oxamate.

Crystal Structure L-Lactate Dehydrogenase A interacting with inhibitor, Oxamate

Drag the structure with the mouse to rotate

References

[12] [13] [14] [15] [16] [17]

  1. ↑ Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science. 2009 May 22;324(5930):1029-33. doi: 10.1126/science.1160809. PMID:19460998 doi:http://dx.doi.org/10.1126/science.1160809
  2. ↑ Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science. 2009 May 22;324(5930):1029-33. doi: 10.1126/science.1160809. PMID:19460998 doi:http://dx.doi.org/10.1126/science.1160809
  3. ↑ Cahn RD, Zwilling E, Kaplan NO, Levine L. Nature and Development of Lactic Dehydrogenases: The two major types of this enzyme form molecular hybrids which change in makeup during development. Science. 1962 Jun 15;136(3520):962-9. doi: 10.1126/science.136.3520.962. PMID:17796806 doi:http://dx.doi.org/10.1126/science.136.3520.962
  4. ↑ Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science. 2009 May 22;324(5930):1029-33. doi: 10.1126/science.1160809. PMID:19460998 doi:http://dx.doi.org/10.1126/science.1160809
  5. ↑ 10.1007/s13277-013-0679-1
  6. ↑ Cahn RD, Zwilling E, Kaplan NO, Levine L. Nature and Development of Lactic Dehydrogenases: The two major types of this enzyme form molecular hybrids which change in makeup during development. Science. 1962 Jun 15;136(3520):962-9. doi: 10.1126/science.136.3520.962. PMID:17796806 doi:http://dx.doi.org/10.1126/science.136.3520.962
  7. ↑ Eventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH. Structural adaptations of lactate dehydrogenase isozymes. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2677-81. PMID:197516
  8. ↑ Poli G, Granchi C, Aissaoui M, Minutolo F, Tuccinardi T. Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors. Molecules. 2017 Dec 13;22(12). pii: molecules22122217. doi:, 10.3390/molecules22122217. PMID:29236080 doi:http://dx.doi.org/10.3390/molecules22122217
  9. ↑ Poli G, Granchi C, Aissaoui M, Minutolo F, Tuccinardi T. Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors. Molecules. 2017 Dec 13;22(12). pii: molecules22122217. doi:, 10.3390/molecules22122217. PMID:29236080 doi:http://dx.doi.org/10.3390/molecules22122217
  10. ↑ Poli G, Granchi C, Aissaoui M, Minutolo F, Tuccinardi T. Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors. Molecules. 2017 Dec 13;22(12). pii: molecules22122217. doi:, 10.3390/molecules22122217. PMID:29236080 doi:http://dx.doi.org/10.3390/molecules22122217
  11. ↑ Poli G, Granchi C, Aissaoui M, Minutolo F, Tuccinardi T. Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors. Molecules. 2017 Dec 13;22(12). pii: molecules22122217. doi:, 10.3390/molecules22122217. PMID:29236080 doi:http://dx.doi.org/10.3390/molecules22122217
  12. ↑ Poli G, Granchi C, Aissaoui M, Minutolo F, Tuccinardi T. Three-Dimensional Analysis of the Interactions between hLDH5 and Its Inhibitors. Molecules. 2017 Dec 13;22(12). pii: molecules22122217. doi:, 10.3390/molecules22122217. PMID:29236080 doi:http://dx.doi.org/10.3390/molecules22122217
  13. ↑ Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science. 2009 May 22;324(5930):1029-33. doi: 10.1126/science.1160809. PMID:19460998 doi:http://dx.doi.org/10.1126/science.1160809
  14. ↑ 10.1007/s13277-013-0679-1
  15. ↑ Eventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH. Structural adaptations of lactate dehydrogenase isozymes. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2677-81. PMID:197516
  16. ↑ Cahn RD, Zwilling E, Kaplan NO, Levine L. Nature and Development of Lactic Dehydrogenases: The two major types of this enzyme form molecular hybrids which change in makeup during development. Science. 1962 Jun 15;136(3520):962-9. doi: 10.1126/science.136.3520.962. PMID:17796806 doi:http://dx.doi.org/10.1126/science.136.3520.962
  17. ↑ doi: https://dx.doi.org/10.1002/mus.880181413
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