Phenylalanine, Tyrosine, and DOPA Are Bona Fide Substrates for Bambusa oldhamii BoPAL4
| Autor: | Chun-Yen Hsieh, Hui-Hsuan Yeh, Che-Jen Hsiao, Yi-Hao Huang, Pei-Yu Hong, Lu-Sheng Hsieh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
biology
Phenylpropanoid Chemistry Stereochemistry substrate specificity Chemical technology Phenylalanine TP1-1185 Phenylalanine ammonia-lyase plant secondary metabolism phenylpropanoid Bambusa oldhamii biology.organism_classification Catalysis chemistry.chemical_compound Yield (chemistry) phenylalanine ammonia-lyase Caffeic acid phenylalanine/tyrosine ammonia-lyase Enzyme kinetics Physical and Theoretical Chemistry QD1-999 Plant secondary metabolism |
| Zdroj: | Catalysts Volume 11 Issue 11 Catalysts, Vol 11, Iss 1263, p 1263 (2021) |
| ISSN: | 2073-4344 |
| DOI: | 10.3390/catal11111263 |
| Popis: | 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-tyrosine, and L-3,4-dihydroxy phenylalanine (L-DOPA) as substrates to yield trans-cinnamic acid, p-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 Km values of BoPAL4 for three substrates were 2084, 98, and 956 μM, respectively. The kcat values of BoPAL4 for three substrates were 1.44, 0.18, and 0.06 σ−1, respectively. The major substrate specificity site mutant, BoPAL4-H123F, showed better affinity toward L-phenylalanine by decreasing its Km value to 640 μM and increasing its kcat value to 1.87 s−1. 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. |
| Databáze: | OpenAIRE |
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