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X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans.

Abstract：

:Thermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43 kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure was solved by molecular replacement method and refined up to 2.14 Å resolution. Structure of the lipase showed an alpha-beta fold with 19 α-helices and 10 β-sheets. The active site remains covered by a lid. One calcium and one zinc atom was found in the crystal. The structure showed a major difference (rmsd 5.6 Å) from its closest homolog in the amino acid region 191 to 203. Thermal unfolding of the lipase showed that the lipase is highly stable with Tm of 76 °C. 13C NMR spectra of products upon triglyceride hydrolysate revealed that the lipase hydrolyses at both sn-1 and sn-2 positions with equal efficiency.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Moharana TR,Pal B,Rao NM

doi

10.1016/j.bbrc.2018.11.105

subject

Has Abstract

pub_date

2019-01-01 00:00:00

pages

145-151

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)32531-2

journal_volume

508

pub_type

杂志文章

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