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Thirty-degree shift in optimum temperature of a thermophilic lipase by a single-point mutation: effect of serine to threonine mutation on structural flexibility.

Abstract：

:In order to understand the molecular basis of cold adaptation, we have used directed evolution to transform a thermophilic lipase LipR1 into its psychrophilic counterpart. A single round of random mutagenesis followed by screening for improved variants yielded a mutant with single-point mutation LipR1M1 (S130T), with optimum activity at 20 °C. Its activity at 50 °C is only 20% as compared to wild type (100%). It showed catalytic rate constant (k cat) 3 times higher and a catalytic efficiency (k cat/K m) 4 times that of wild type. Circular dichroism and fluorescence studies also supported our observation of mutant structural flexibility. Structure analysis using homology models showed that Threonine 130 is exposed to solvent and has lost H-bond interaction with neighboring amino acid, thereby increasing flexibility of this lipase structure.

journal_name

Mol Cell Biochem

journal_title

Molecular and cellular biochemistry

authors

Sharma M,Kumar R,Singh R,Kaur J

doi

10.1007/s11010-017-2950-z

subject

Has Abstract

pub_date

2017-06-01 00:00:00

pages

21-30

issue

1-2

eissn

0300-8177

issn

1573-4919

pii

10.1007/s11010-017-2950-z

journal_volume

430

pub_type

杂志文章

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