4HS9
Methanol tolerant mutant of the Proteus mirabilis lipase
Summary for 4HS9
| Entry DOI | 10.2210/pdb4hs9/pdb |
| Related | 4GW3 4GXN |
| Descriptor | Lipase, CALCIUM ION, CHLORIDE ION, ... (7 entities in total) |
| Functional Keywords | lipase, hydrolase, alpha/beta hydrolase |
| Biological source | Proteus mirabilis |
| Total number of polymer chains | 1 |
| Total formula weight | 34673.42 |
| Authors | Korman, T.P. (deposition date: 2012-10-29, release date: 2013-05-22, Last modification date: 2024-10-16) |
| Primary citation | Korman, T.P.,Sahachartsiri, B.,Charbonneau, D.M.,Huang, G.L.,Beauregard, M.,Bowie, J.U. Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution. Biotechnol Biofuels, 6:70-70, 2013 Cited by PubMed Abstract: Biodiesels are methyl esters of fatty acids that are usually produced by base catalyzed transesterification of triacylglyerol with methanol. Some lipase enzymes are effective catalysts for biodiesel synthesis and have many potential advantages over traditional base or acid catalyzed transesterification. Natural lipases are often rapidly inactivated by the high methanol concentrations used for biodiesel synthesis, however, limiting their practical use. The lipase from Proteus mirabilis is a particularly promising catalyst for biodiesel synthesis as it produces high yields of methyl esters even in the presence of large amounts of water and expresses very well in Escherichia coli. However, since the Proteus mirabilis lipase is only moderately stable and methanol tolerant, these properties need to be improved before the enzyme can be used industrially. PubMed: 23648063DOI: 10.1186/1754-6834-6-70 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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