Document Detail

Characterization of a novel l-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027.
MedLine Citation:
PMID:  24333187     Owner:  NLM     Status:  Publisher    
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, N(α)-benzyloxycarbonyl-l-lysine (N(α)-Z-l-lysine) and N(ε)-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 N(α)-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.
Kimiyasu Isobe; Ryota Taira; Youko Hoshi; Sou Matsuda; Miwa Yamada; Makoto Hibi; Shigenobu Kishino; Jun Ogawa
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-12-12
Journal Detail:
Title:  Journal of bioscience and bioengineering     Volume:  -     ISSN:  1347-4421     ISO Abbreviation:  J. Biosci. Bioeng.     Publication Date:  2013 Dec 
Date Detail:
Created Date:  2013-12-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888800     Medline TA:  J Biosci Bioeng     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
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