Lactate dehydrogenase b

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Lactate dehydrogenase B (LDHB) is an enzyme that is primarily found in the heart and muscle tissues. It is one of the two subunits that make up the lactate dehydrogenase (LDH) enzyme, the other being lactate dehydrogenase A (LDHA). LDHB is encoded by the LDHB gene.

Function[edit | edit source]

LDHB is involved in the conversion of lactate to pyruvate, a critical step in the metabolic pathway known as glycolysis. This process is essential for the production of adenosine triphosphate (ATP), the main energy source for cells. LDHB has a higher affinity for pyruvate, allowing it to function more efficiently in conditions where oxygen is abundant.

Structure[edit | edit source]

The LDHB subunit is composed of 334 amino acids and has a molecular weight of approximately 37 kDa. The LDHB gene is located on the short (p) arm of chromosome 12 at position 12. The structure of LDHB is similar to that of LDHA, but there are key differences in their amino acid sequences that account for their different enzymatic properties.

Clinical significance[edit | edit source]

Alterations in the LDHB gene can lead to a decrease in LDHB enzyme activity, which can result in a variety of medical conditions. For example, mutations in the LDHB gene have been associated with hereditary LDH deficiency, a rare condition characterized by muscle rigidity and weakness. Additionally, elevated levels of LDHB have been observed in certain types of cancer, suggesting a potential role for this enzyme in tumor progression.

See also[edit | edit source]

References[edit | edit source]


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Contributors: Prab R. Tumpati, MD