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From Proteopedia
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The lysosome is a membrane-bound organelle which is present in animal cells. those are acidic vesicles and contain more than fifty digestive enzymes as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, acidic pH is important for the degradation of intracellular and extracellular compounds. | The lysosome is a membrane-bound organelle which is present in animal cells. those are acidic vesicles and contain more than fifty digestive enzymes as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, acidic pH is important for the degradation of intracellular and extracellular compounds. | ||
| - | Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: phospholipases. These phospholipases are classified into four types, phospholipase A1, A2, C and D depending on the specific cleavage site of the substrate. | + | Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: phospholipases. These phospholipases are classified into four types, phospholipase A1, A2, C and D depending on the specific cleavage site of the substrate. Phospholipase A2 cleave the acyl-ester bonds of sn-2 position of glycerophospholipids and they produce free fatty acids. |
| - | Phospholipase A2 cleave the acyl-ester bonds of sn-2 position of glycerophospholipids and they produce free fatty acids. | + | |
Revision as of 17:34, 22 January 2017
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
