Stereoselectivity of Mucorales lipases toward triradylglycerols—A simple solution to a complex problem

• Published in: Protein science Vol. 8; no. 1; pp. 215 - 221
• Main Authors: SCHEIB, HOLGER, PLEISS, JÜRGEN, KOVAC, ANDREA, PALTAUF, FRITZ, SCHMID, ROLF D.
• Format: Journal Article
• Language: English
• Published: Bristol Cambridge University Press 01.01.1999; Cold Spring Harbor Laboratory Press
• Subjects: Amino Acid Sequence; Binding Sites; Glycerol - metabolism; G‐elbow loop; His gap; Lipase - chemistry; Lipase - metabolism; Models, Molecular; Molecular Probes; Molecular Sequence Data; Mucorales - enzymology; Mucorales lipase; Protein Conformation; protein engineering; Sequence Homology, Amino Acid; stereoselectivity; triradylglycerol substrate; protein engineering; stereoselectivity; triradylglycerol substrate; G-elbow loop; Mucorales lipase; His gap; model

The lipases from Rhizopus and Rhizomucor are members of the family of Mucorales lipases. Although they display high sequence homology, their stereoselectivity toward triradylglycerols (sn-2 substituted triacylglycerols) varies. Four different triradylglycerols were investigated, which were classifie...