PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution

Abstract D-amino acid oxidases (DAAO) are stereospecific enzymes which are generally almost inactive towards L-enantiomer in neutral solution when L-, D-amino acids are supplied as substrates. In this paper, the D-amino acid oxidase can catalytic oxidize L-amino acids by modulating pH of aqueous sol...

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Autores principales:	Qingju Liu, Li Chen, Zhikun Zhang, Bibai Du, Yating Xiao, Kunhao Yang, Lingling Gong, Li Wu, Xiangjun Li, Yujian He
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/366929d02861413da266a82bc9d372c9
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spelling	oai:doaj.org-article:366929d02861413da266a82bc9d372c92021-12-02T12:31:47ZPH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution10.1038/s41598-017-03177-y2045-2322https://doaj.org/article/366929d02861413da266a82bc9d372c92017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03177-yhttps://doaj.org/toc/2045-2322Abstract D-amino acid oxidases (DAAO) are stereospecific enzymes which are generally almost inactive towards L-enantiomer in neutral solution when L-, D-amino acids are supplied as substrates. In this paper, the D-amino acid oxidase can catalytic oxidize L-amino acids by modulating pH of aqueous solution. With L-Pro as substrate, the catalytic rate (k cat) and the affinity (K m) of DAAO were 6.71 s−1 and 33 mM at pH 8.0, respectively, suggesting that optimal pH condition enhanced the activity of DAAO towards L-Pro. Similar results were obtained when L-Ala (pH 9.8), L-Arg (pH 6.5), L-Phe (pH 9.0), L-Thr (pH 9.4), and L-Val (pH 8.5) were catalyzed by DAAO at various pH values. The racemization of the L-amino acids was not found by capillary electrophoresis analysis during oxidation, and quantification analysis of L-amino acids before and after catalytic reaction was performed, which confirmed that the modulation of enantioselectivity of DAAO resulted from the oxidation of L-amino acids rather than D-amino acids by changing pH. A mechanistic model was proposed to explain enhanced activity of DAAO towards L-amino acids under optimal pH condition.Qingju LiuLi ChenZhikun ZhangBibai DuYating XiaoKunhao YangLingling GongLi WuXiangjun LiYujian HeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Qingju Liu Li Chen Zhikun Zhang Bibai Du Yating Xiao Kunhao Yang Lingling Gong Li Wu Xiangjun Li Yujian He PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
description	Abstract D-amino acid oxidases (DAAO) are stereospecific enzymes which are generally almost inactive towards L-enantiomer in neutral solution when L-, D-amino acids are supplied as substrates. In this paper, the D-amino acid oxidase can catalytic oxidize L-amino acids by modulating pH of aqueous solution. With L-Pro as substrate, the catalytic rate (k cat) and the affinity (K m) of DAAO were 6.71 s−1 and 33 mM at pH 8.0, respectively, suggesting that optimal pH condition enhanced the activity of DAAO towards L-Pro. Similar results were obtained when L-Ala (pH 9.8), L-Arg (pH 6.5), L-Phe (pH 9.0), L-Thr (pH 9.4), and L-Val (pH 8.5) were catalyzed by DAAO at various pH values. The racemization of the L-amino acids was not found by capillary electrophoresis analysis during oxidation, and quantification analysis of L-amino acids before and after catalytic reaction was performed, which confirmed that the modulation of enantioselectivity of DAAO resulted from the oxidation of L-amino acids rather than D-amino acids by changing pH. A mechanistic model was proposed to explain enhanced activity of DAAO towards L-amino acids under optimal pH condition.
format	article
author	Qingju Liu Li Chen Zhikun Zhang Bibai Du Yating Xiao Kunhao Yang Lingling Gong Li Wu Xiangjun Li Yujian He
author_facet	Qingju Liu Li Chen Zhikun Zhang Bibai Du Yating Xiao Kunhao Yang Lingling Gong Li Wu Xiangjun Li Yujian He
author_sort	Qingju Liu
title	PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
title_short	PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
title_full	PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
title_fullStr	PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
title_full_unstemmed	PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution
title_sort	ph-dependent enantioselectivity of d-amino acid oxidase in aqueous solution
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/366929d02861413da266a82bc9d372c9
work_keys_str_mv	AT qingjuliu phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT lichen phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT zhikunzhang phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT bibaidu phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT yatingxiao phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT kunhaoyang phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT linglinggong phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT liwu phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT xiangjunli phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution AT yujianhe phdependentenantioselectivityofdaminoacidoxidaseinaqueoussolution
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PH-Dependent Enantioselectivity of D-amino Acid Oxidase in Aqueous Solution

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