Heptadecanoyl Coenzyme A
Modify Date: 2024-01-07 17:35:12
Heptadecanoyl Coenzyme A structure
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Common Name | Heptadecanoyl Coenzyme A | ||
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| CAS Number | 3546-17-6 | Molecular Weight | 1019.97000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C38H68N7O17P3S | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
Use of Heptadecanoyl Coenzyme AHeptadecanoyl Coenzyme A (Heptadecanoyl-CoA), long-chain acyl-coenzymes A (acyl-CoAs) (LCACoA), is an intermediate in lipid metabolism. Heptadecanoyl Coenzyme A can be used for the research of glucose metabolism[1]. |
| Name | heptadecanoyl-CoA |
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| Synonym | More Synonyms |
| Description | Heptadecanoyl Coenzyme A (Heptadecanoyl-CoA), long-chain acyl-coenzymes A (acyl-CoAs) (LCACoA), is an intermediate in lipid metabolism. Heptadecanoyl Coenzyme A can be used for the research of glucose metabolism[1]. |
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| Related Catalog | |
| References |
| Molecular Formula | C38H68N7O17P3S |
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| Molecular Weight | 1019.97000 |
| Exact Mass | 1019.36000 |
| PSA | 418.36000 |
| LogP | 5.89910 |
| Personal Protective Equipment | Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter |
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| RIDADR | NONH for all modes of transport |
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Evidence for two-step regulation of pheromone biosynthesis by the pheromone biosynthesis-activating neuropeptide in the moth Heliothis virescens.
Arch. Insect Biochem. Physiol. 64 , 120-130, (2007) The control of pheromone biosynthesis by the neuropeptide PBAN was investigated in the moth Heliothis virescens. When decapitated females were injected with [2-(14)C] acetate, females co-injected with... |
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Improved and simplified tissue extraction method for quantitating long-chain acyl-coenzyme A thioesters with picomolar detection using high-performance liquid chromatography.
J. Chromatogr. A. 577 , 157-162, (1992) A method has been developed that permits rapid and easy tissue extraction of long-chain acyl-coenzyme A (acyl-CoA) thioesters with sensitive quantitation by reversed-phase high-performance liquid chro... |
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Modification of an arginine residue in pig kidney general acyl-coenzyme A dehydrogenase by cyclohexane-1,2-dione.
Biochem. J. 207 , 415-419, (1982) The flavoenzyme pig kidney general acyl-CoA dehydrogenase (EC 1.3.99.3) is inactivated by cyclohexane-1,2-dione in borate buffer in a reaction that exhibits pseudo-first-order kinetics. Strong protect... |
| MFCD00079338 |