2014年6月
Characterization of a novel L-amino acid oxidase with protein oxidizing activity from Penicillium steckii AIU 027
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
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- 巻
- 117
- 号
- 6
- 開始ページ
- 690
- 終了ページ
- 695
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.jbiosc.2013.11.008
- 出版者・発行元
- SOC BIOSCIENCE BIOENGINEERING JAPAN
An enzyme exhibiting oxidase activity for beta-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-alpha-benzylox-ycarbonyl-L-lysine (N-alpha-Z-L-lysine) and N-epsilon-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 a-amino group and the e-amino group in i.-amino acids and L-lysine-containing peptides, and the values for L-lysine-containing polypeptides were lower than those for N-alpha-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, ENIAD-VADAMGPWFDGVAYMKSKKN, 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. (C) 2013, The Society for Biotechnology, Japan. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.jbiosc.2013.11.008
- ISSN : 1389-1723
- eISSN : 1347-4421
- Web of Science ID : WOS:000339219400007