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Characterization of a novel l-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027

Paper ID Volume ID Publish Year Pages File Format Full-Text
20639 43184 2014 6 PDF Available
Title
Characterization of a novel l-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027
Abstract

An enzyme exhibiting oxidase activity for β-lactoglobulin, myoglobin, and l-lysine-containing peptides was found from a newly isolated fungal strain, Penicillium steckii AIU 027. The enzyme also oxidized l-amino acids, Nα-benzyloxycarbonyl-l-lysine (Nα-Z-l-lysine) and Nε-Z-l-lysine, but not d-amino acids and amines. Thus, the enzyme was classified into a group of l-amino acid oxidases (l-AAOs). However, characteristics of this l-AAO were significantly different from those of other l-AAOs as follows. The l-AAO from P. steckii AIU 027 oxidized both the α-amino group and the ε-amino group in l-amino acids and l-lysine-containing peptides, and the Km values for l-lysine-containing polypeptides were lower than those for Nα-Z-l-lysine and l-lysine-containing dipeptides. The enzyme contained flavin and iron, and composed of four identical subunits with molecular mass of 75.3 kDa. The N-terminal amino acid sequence, ENIADVADAMGPWFDGVAYMKSKKN, was different from that of other l-AAOs. Thus, the l-AAO with protein oxidase activity was first reported here from P. steckii AIU 027.

Keywords
l-Amino acid oxidase; Protein oxidase; l-Lysine; Lysyl oxidase; Penicillium steckii
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Characterization of a novel l-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 117, Issue 6, June 2014, Pages 690–695
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
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