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Biochemical characterization of a metagenome-derived decarboxylase

Paper ID Volume ID Publish Year Pages File Format Full-Text
17543 42676 2009 6 PDF Available
Title
Biochemical characterization of a metagenome-derived decarboxylase
Abstract

The metagenomic library screening approach has broadened the field of enzymology, leading to the identification of a wider range of natural biocatalysts. Based on cloning a novel cysteine decarboxylase gene (undec1A) from soil metagenome, we presented a detailed study of the biochemical properties of the recombinant Undec1A protein with a high performance liquid chromatography method and automatic amino acid analyzer method using l-cysteine as the substrate. We found that the maximum activity for the decarboxylase occurred at pH 7.0 and 35 °C. The decarboxylase had an apparent Km value of 0.59 mM, a Vmax value of 68.5 μM/min and a kcat value of 4.57/min. We demonstrated that the active catalytic domain of Undec1A protein contained a potential Mg2+ binding site. Furthermore, through mutation analysis we found that the amino acid residues of His-30 in His insertion motif and Ser-113 in ACGD motif were necessary for the activity of Undec1A protein. The characterization of the biochemical properties of Undec1A enhanced our understanding of this novel decarboxylase isolated from uncultured soil microorganisms.

Keywords
Biocatalyst; Soil metagenome; Decarboxylase; Biochemical properties
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Biochemical characterization of a metagenome-derived decarboxylase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 45, Issue 1, 8 July 2009, Pages 58–63
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us