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中国生物工程杂志

CHINA BIOTECHNOLOGY
中国生物工程杂志  2012, Vol. 32 Issue (03): 125-135    
综述     
L-氨基酸氧化酶的研究进展
余志良, 周宁, 乔华
浙江工业大学生物与环境工程学院 杭州 310014
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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摘要:

L-氨基酸氧化酶(L-amino acid oxidase, LAAO)能特异性催化L-氨基酸氧化脱氨,生成α-酮酸、氨和H2O2。该酶分布较广,其中蛇毒源LAAO是该类酶中研究最为深入的一类,近年来,越来越多的非蛇毒源LAAO被发现和报道,现对蛇毒源和非蛇毒源LAAO的研究进展进行了综述。现有研究表明,不同物种来源的LAAO,其底物选择性、等电点、稳定性等理化性质不尽相同;虽对其结构的研究还较少,但现有的研究表明蛇毒源和非蛇毒源LAAO的结构都含有FAD结合结构域、底物结构域和螺旋结构域;研究已发现不同来源的LAAO体外具有多种不同的生物学功能,而这些生物学功能多数是由于其产物H2O2作用的结果;对LAAO异源表达的研究较少且都不甚成功,可能是由于其需要进行翻译后修饰。

关键词: L-氨基酸氧化酶生理生化和结构特征生物学功能异源表达    
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 words: LAAO    Physiological and structural properties    Biological functions    Heterologous expression
收稿日期: 2011-09-20 出版日期: 2012-03-25
ZTFLH:  Q55  
基金资助:

浙江省自然科学基金(Y5100153)、浙江省公益性应用研究计划(2011C23007)资助项目

通讯作者: 余志良,zlyu@zjut.edu.cn     E-mail: zlyu@zjut.edu.cn
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余志良, 周宁, 乔华. L-氨基酸氧化酶的研究进展[J]. 中国生物工程杂志, 2012, 32(03): 125-135.

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

链接本文:

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


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