Enzymes for Research, Diagnostic and Industrial Use
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| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| NATE-0568 | Native Rabbit Pyruvate Kinase/Lactic Dehydrogenase enzymes | rabbit muscle | Inquiry |
Enzymes play a crucial role in biological systems, catalyzing a vast array of biochemical reactions essential for life. The focus on PK/LDH enzymes offers a fascinating insight into the intricate mechanisms involved in cellular metabolism. They are typically proteins that exhibit remarkable specificity for their substrates, ensuring that reactions proceed efficiently and accurately. PK and LDH enzymes are two such critical players in cellular metabolism, influencing pathways essential for energy production and maintaining cellular homeostasis.
Pyruvate kinase is an enzyme involved in the final step of glycolysis, a central pathway for glucose metabolism. PK catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), generating pyruvate and ATP. This reaction is pivotal for energy generation, as ATP serves as the primary energy currency of the cell. PK exists in various isoforms, with tissue-specific differences in structure and regulation. For instance, the PK isozymes M1 and M2 are found in muscle and liver tissues, respectively, reflecting their distinct roles in energy metabolism and biosynthetic pathways. The regulation of PK activity is finely tuned by allosteric effectors, post-translational modifications, and gene expression, ensuring that glycolytic flux is modulated according to cellular demands.
Lactate dehydrogenase is another key enzyme involved in cellular metabolism, particularly in anaerobic conditions where oxygen availability is limited. LDH catalyzes the interconversion of pyruvate and lactate, utilizing NADH as a cofactor in this reversible reaction. This process helps regenerate NAD+ for continued glycolytic flux, ensuring that energy production can be sustained even in the absence of oxygen. LDH is a tetrameric enzyme composed of subunits that can assemble into different isoforms, each with distinct kinetic properties and tissue distributions. The LDH enzyme plays a crucial role in maintaining redox balance within cells, regulating lactate levels, and adapting metabolism to varying oxygen conditions.
The interconnectedness of PK and LDH enzymes underscores their collaborative roles in cellular metabolism. PK generates pyruvate, a key substrate for LDH, which in turn influences lactate production and redox balance. This dynamic relationship between glycolytic enzymes highlights the complexity of metabolic regulation and the need for precise coordination to maintain energy homeostasis. The regulation of PK and LDH activities is intricately linked to cellular signaling pathways, metabolic demands, and environmental cues. Transcriptional regulation, post-translational modifications, and allosteric modulation are mechanisms through which cells fine-tune the activities of these enzymes, ensuring metabolic flexibility and responsiveness to changing conditions.
The dysregulation of PK and LDH enzymes has profound implications for human health and disease. Mutations in PK genes are associated with metabolic disorders like pyruvate kinase deficiency and hemolytic anemia, emphasizing the importance of these enzymes in red blood cell function and energy metabolism. LDH has been implicated in various pathological conditions, including cardiovascular diseases, neurodegenerative disorders, and cancer. Altered LDH expression and activity contribute to metabolic reprogramming in cancer cells, driving proliferation and metastasis. Targeting LDH activity presents a promising avenue for developing novel cancer therapies that exploit metabolic vulnerabilities in tumor cells.
