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1 Holmquist M, "Trp89 in the lid of Humicola lanuginosa lipase is important for efficient hydrolysis of tributyrin" 29 : 599-603, 1994
2 Noble ME, "The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate" 331 : 123-128, 1993
3 Tang L, "Substitution of Val72 residue alters the enantioselectivity and activity of Penicillium expansum lipase" 29 : 145-151, 2013
4 Shih TW, "Substitution of Asp189 residue alters the activity and thermostability of Geobacillus sp. NTU 03 lipase" 33 : 1841-1846, 2011
5 Brzozowski AM, "Structural origins of the interfacial activation in Thermomyces (Humicola)lanuginosa lipase" 39 : 15071-15082, 2000
6 Gao CL, "Site-directed mutagenesis studies of the aromatic residues at the active site of a lipase from Malassezia globosa" 102 : 29-36, 2014
7 Brocca S, "Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes" 12 : 2312-2319, 2003
8 Wang WF, "Production of lipase SMG1 and its application in synthesizing diacylglyecrol" 77 : 87-91, 2012
9 Schuttelkopf AW, "PRODRG: a tool for high-throughput crystallography of protein-ligand complexes" 60 : 1355-1363, 2004
10 Martinelle M, "On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase" 1258 : 272-276, 1995
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26 Brady L, "A serine protease triad forms the catalytic centre of a triacylglycerol lipase" 343 : 767-770, 1990
27 Verger R., "'Interfacial activation' of lipases: facts and artifacts" 15 : 32-38, 1997