9075-65-4
Chemical Structure
Glycerol-3-phosphate dehydrogenase, rabbit muscle
Synonym(s): GPDH, rabbit muscle; α-Glycerophosphate dehydrogenase, rabbit muscle; Glycerol phosphate dehydrogenase, rabbit muscle
- CAS No.: 9075-65-4
- Formula:N/A
- Molecular Weight:N/A
SMILES: [Glycerol-3-phosphate dehydrogenase, rabbit muscle]
Biological Activity: Glycerol‑3‑phosphate dehydrogenase, rabbit muscle (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from rabbit muscle that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle uses NADH as a reducing equivalent donor, and its substrate binding relies on the phosphate-binding site in the active center; it catalyzes the reversible reduction of dihydroxyacetone phosphate to L‑α‑glycerol‑3‑phosphate. The catalytic activity of the enzymatic reaction of Glycerol‑3‑phosphate dehydrogenase, rabbit muscle is regulated by pH and divalent metal ions. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle can be used in metabolism-related studies[1][2].
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Glycerol-3-phosphate dehydrogenase, rabbit muscle | Glycerol‑3‑phosphate dehydrogenase, rabbit muscle (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from rabbit muscle that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle uses NADH as a reducing equivalent donor, and its substrate binding relies on the phosphate-binding site in the active center; it catalyzes the reversible reduction of dihydroxyacetone phosphate to L‑α‑glycerol‑3‑phosphate. The catalytic activity of the enzymatic reaction of Glycerol‑3‑phosphate dehydrogenase, rabbit muscle is regulated by pH and divalent metal ions. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle can be used in metabolism-related studies. | |||||||||||||||||||||
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Glycerol-3-phosphate dehydrogenase, microorganism | Glycerol-3-phosphate dehydrogenase, microorganism (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from microorganism that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol-3-phosphate dehydrogenase, microorganism uses NADH as a reducing equivalent donor, and its substrate binding relies on the phosphate-binding site in the active center; it catalyzes the reversible reduction of dihydroxyacetone phosphate to L‑α‑glycerol‑3‑phosphate. The catalytic activity of the enzymatic reaction of Glycerol-3-phosphate dehydrogenase, microorganism is regulated by pH and divalent metal ions. Glycerol-3-phosphate dehydrogenase, microorganism can be used in metabolism-related studies. | |||||||||||||||||||||
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References
- [1]. Harris J I. GLYCERALDEHYDE 3‑PHOSPHATE DEHYDROGENASE. In: Structure and Function of Oxidation‑Reduction Enzymes, Proceedings of the Wenner‑Gren Symposium Held at the Wenner‑Gren Center, Stockholm, 23‑27 August, 1970. 1972: 639‑645.
- [2]. Chuang DM, et al. Glyceraldehyde-3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases. Annual review of pharmacology and toxicology. 2005;45:269-90.
