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中国生物工程杂志

China Biotechnology
China Biotechnology  2012, Vol. 32 Issue (03): 125-135    DOI:
    
Advances in L-amino Acid Oxidase
YU Zhi-liang, ZHOU Ning, QIAO Hua
College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou 310014, China
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Abstract  

L-amino acid oxidase is dimeric flavoprotein, and each subunit contains a non-covalently bound FAD molecule as cofactor. It is able to catalyze the stereospecific oxidative deamination of L-amino acids to the corresponding a-imino acids which are then hydrolyzed to corresponding a-keto acids with release of NH4+, along with two electrons transferring from the amino acid to the flavin cofactor which subsequently reduces molecular oxygen to H2O2. This enzyme is widely distributed in nature. So far snake venom LAAO is the best characterized member of this enzyme family. Recently, non-snake venom LAAOs have increasingly been found. Current researches show that different LAAOs have different physiological properties, including substrate specificity, pI value, and storage stability. Little is known about its structure, but the structures of both snake venom and non-snake venom LAAOs indicate that it all consists of FAD-binding domain, substrate-binding domain and helical domain. LAAO has various biological functions which are found to be probably related to the produced-H2O2. Probably due to post-translational modification of LAAO, only some heterologous expression systems have been reported hitherto.



Key wordsLAAO      Physiological and structural properties      Biological functions      Heterologous expression     
Received: 20 September 2011      Published: 25 March 2012
ZTFLH:  Q55  
Cite this article:

YU Zhi-liang, ZHOU Ning, QIAO Hua. Advances in L-amino Acid Oxidase. China Biotechnology, 2012, 32(03): 125-135.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2012/V32/I03/125


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