Phenylalanine, Tyrosine, and DOPA Are bona fide Substrates for Bambusa oldhamii BoPAL4

Phenylalanine ammonia-lyase (PAL) links the plant primary and secondary metabolisms, and its product, trans-cinnamic acid, is derived into thousands of diverse phenylpropanoids. Bambusa oldhamii BoPAL4 has broad substrate specificity using L-phenylalanine, L-tyr...

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Autores principales:	Chun-Yen Hsieh, Yi-Hao Huang, Hui-Hsuan Yeh, Pei-Yu Hong, Che-Jen Hsiao, Lu-Sheng Hsieh
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	<i>Bambusa oldhamii</i> phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase substrate specificity plant secondary metabolism phenylpropanoid Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/edff940881e3468eb933fd6d250d3729
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spelling	oai:doaj.org-article:edff940881e3468eb933fd6d250d37292021-11-25T17:05:07ZPhenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL410.3390/catal111112632073-4344https://doaj.org/article/edff940881e3468eb933fd6d250d37292021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1263https://doaj.org/toc/2073-4344Phenylalanine ammonia-lyase (PAL) links the plant primary and secondary metabolisms, and its product, <i>trans</i>-cinnamic acid, is derived into thousands of diverse phenylpropanoids. <i>Bambusa oldhamii</i> BoPAL4 has broad substrate specificity using L-phenylalanine, L-tyrosine, and L-3,4-dihydroxy phenylalanine (L-DOPA) as substrates to yield <i>trans</i>-cinnamic acid, <i>p</i>-coumaric acid, and caffeic acid, respectively. The optimum reaction pH of BoPAL4 for three substrates was measured at 9.0, 8.5, and 9.0, respectively. The optimum reaction temperatures of BoPAL4 for three substrates were obtained at 50, 60, and 40 °C, respectively. The <i>K</i>m values of BoPAL4 for three substrates were 2084, 98, and 956 μM, respectively. The <i>k</i><sub>cat</sub> values of BoPAL4 for three substrates were 1.44, 0.18, and 0.06 σ<sup>−1</sup>, respectively. The major substrate specificity site mutant, BoPAL4-H123F, showed better affinity toward L-phenylalanine by decreasing its <i>K</i><sub>m</sub> value to 640 μM and increasing its <i>k</i><sub>cat</sub> value to 1.87 s<sup>−1</sup>. In comparison to wild-type BoPAL4, the specific activities of BoPAL4-H123F using L-tyrosine and L-DOPA as substrates retained 5.4% and 17.8% residual activities. Therefore, L-phenylalanine, L-tyrosine, and L-DOPA are bona fide substrates for BoPAL4.Chun-Yen HsiehYi-Hao HuangHui-Hsuan YehPei-Yu HongChe-Jen HsiaoLu-Sheng HsiehMDPI AGarticle<i>Bambusa oldhamii</i>phenylalanine ammonia-lyasephenylalanine/tyrosine ammonia-lyasesubstrate specificityplant secondary metabolismphenylpropanoidChemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1263, p 1263 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	<i>Bambusa oldhamii</i> phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase substrate specificity plant secondary metabolism phenylpropanoid Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	<i>Bambusa oldhamii</i> phenylalanine ammonia-lyase phenylalanine/tyrosine ammonia-lyase substrate specificity plant secondary metabolism phenylpropanoid Chemical technology TP1-1185 Chemistry QD1-999 Chun-Yen Hsieh Yi-Hao Huang Hui-Hsuan Yeh Pei-Yu Hong Che-Jen Hsiao Lu-Sheng Hsieh Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
description	Phenylalanine ammonia-lyase (PAL) links the plant primary and secondary metabolisms, and its product, <i>trans</i>-cinnamic acid, is derived into thousands of diverse phenylpropanoids. <i>Bambusa oldhamii</i> BoPAL4 has broad substrate specificity using L-phenylalanine, L-tyrosine, and L-3,4-dihydroxy phenylalanine (L-DOPA) as substrates to yield <i>trans</i>-cinnamic acid, <i>p</i>-coumaric acid, and caffeic acid, respectively. The optimum reaction pH of BoPAL4 for three substrates was measured at 9.0, 8.5, and 9.0, respectively. The optimum reaction temperatures of BoPAL4 for three substrates were obtained at 50, 60, and 40 °C, respectively. The <i>K</i>m values of BoPAL4 for three substrates were 2084, 98, and 956 μM, respectively. The <i>k</i><sub>cat</sub> values of BoPAL4 for three substrates were 1.44, 0.18, and 0.06 σ<sup>−1</sup>, respectively. The major substrate specificity site mutant, BoPAL4-H123F, showed better affinity toward L-phenylalanine by decreasing its <i>K</i><sub>m</sub> value to 640 μM and increasing its <i>k</i><sub>cat</sub> value to 1.87 s<sup>−1</sup>. In comparison to wild-type BoPAL4, the specific activities of BoPAL4-H123F using L-tyrosine and L-DOPA as substrates retained 5.4% and 17.8% residual activities. Therefore, L-phenylalanine, L-tyrosine, and L-DOPA are bona fide substrates for BoPAL4.
format	article
author	Chun-Yen Hsieh Yi-Hao Huang Hui-Hsuan Yeh Pei-Yu Hong Che-Jen Hsiao Lu-Sheng Hsieh
author_facet	Chun-Yen Hsieh Yi-Hao Huang Hui-Hsuan Yeh Pei-Yu Hong Che-Jen Hsiao Lu-Sheng Hsieh
author_sort	Chun-Yen Hsieh
title	Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
title_short	Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
title_full	Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
title_fullStr	Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
title_full_unstemmed	Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4
title_sort	phenylalanine, tyrosine, and dopa are <i>bona fide</i> substrates for <i>bambusa oldhamii</i> bopal4
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/edff940881e3468eb933fd6d250d3729
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Phenylalanine, Tyrosine, and DOPA Are <i>bona fide</i> Substrates for <i>Bambusa oldhamii</i> BoPAL4

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