NDLI: Manipulation of the Conformation and Enzymatic Properties of T1 Lipase by Site-Directed Mutagenesis of the Protein Core

Content Provider	Springer Nature Link
Author	Wahab, Roswanira Abdul Basri, Mahiran Rahman, Raja or Zaliha Raja Abdul Salleh, Abu Bakar Rahman, Mohd Basyaruddin Abdul Chor, Leow Thean
Copyright Year	2012
Abstract	In silico and experimental investigations were conducted to explore the effects of substituting hydrophobic residues, Val, Met, Leu, Ile, Trp, and Phe into Gln 114 of T1 lipase. The in silico investigations accurately predicted the enzymatic characteristics of the mutants in the experimental studies and provided rationalization for some of the experimental observations. Substitution with Leu successfully improved the conformational stability and enzymatic characteristics of T1 lipase. However, replacement of Gln114 with Trp negatively affected T1 lipase and resulted in the largest disruption of protein stability, diminished lipase activity and inferior enzymatic characteristics. These results suggested that the substitution of a larger residue in a densely packed area of the protein core can have considerable effects on the structure and function of an enzyme. This is especially true when the residue is next to the catalytic serine as demonstrated with the Phe and Trp mutation.
Starting Page	612
Ending Page	620
Page Count	9
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	167
Issue Number	3
e-ISSN	15590291
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-05-12
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Hydrophobic residue Hydrophobic core T1 lipase Protein design Conformational stability Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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