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Semi-rational design improves the catalytic activity of phenylalanine ammonia lyase from Anabaena variabilis
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Xi-yu WEI1, Cui-yue FENG1, Rui-jie LV1, Shuai FAN2, Zhao-yong YANG2, *, Zhi-fei ZHANG1, *
Acta Pharmaceutica Sinica | 2022, 57(12) : 3669 - 3674
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Acta Pharmaceutica Sinica | 2022, 57(12): 3669-3674
• Original Articles •
Semi-rational design improves the catalytic activity of phenylalanine ammonia lyase from Anabaena variabilis
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Xi-yu WEI1, Cui-yue FENG1, Rui-jie LV1, Shuai FAN2, Zhao-yong YANG2, *, Zhi-fei ZHANG1, *
Affiliations
  • 1. School of Pharmacy, North China University of Science and Technology, Tangshan 063200, China
  • 2. Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China
Published: 2022-12-12 doi: 10.16438/j.0513-4870.2022-0631
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Phenylalanine ammonia lyase (PAL) can catalyze L-phenylalanine to produce trans-cinnamic acid, which is widely used in the fields of pharmacy, food and agriculture. In particular, phenylalanine ammonia lyase from Anabaena variabilis (AvPAL) is the only protein drug for the treatment of phenylketonuria. However, the poor activity and low stability limit the application in industry of AvPAL. In this study, the key amino acids of substrate-binding cavity in AvPAL were identified by screening the single site saturation mutagenesis library. Subsequently, the impact of replacing M222 with the additional 19 amino acids on activity was also evaluated by site-directed mutagenesis. It was found that the kcat values of mutants M222L and M222V were 90% and 60% higher than that of AvPAL, and the kcat/Km was 1.4 and 1.5 times as that of AvPAL. Molecular docking results revealed that the higher activity of M222L and M222V may be due to the increase of hydrophobicity favorable for the substrate-binding cavity. This study is important for elucidating the structure-function relationship of AvPAL.

phenylalanine ammonia lyase  /  saturation mutation  /  catalytic efficiency  /  molecular docking
Xi-yu WEI, Cui-yue FENG, Rui-jie LV, Shuai FAN, Zhao-yong YANG, Zhi-fei ZHANG. Semi-rational design improves the catalytic activity of phenylalanine ammonia lyase from Anabaena variabilis[J]. Acta Pharmaceutica Sinica, 2022 , 57 (12) : 3669 -3674 . DOI: 10.16438/j.0513-4870.2022-0631
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Year 2022 volume 57 Issue 12
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Article Info
doi: 10.16438/j.0513-4870.2022-0631
  • Receive Date：2022-05-25
  • Online Date：2025-12-24
  • Published：2022-12-12
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  • Received：2022-05-25
  • Revised：2022-06-07
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Affiliations
    1. School of Pharmacy, North China University of Science and Technology, Tangshan 063200, China
    2. Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China
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表12种不同金属材料的力学参数
科
Family		 属数
Number of
genus		 种数
Number of
species		 占总种数比例
Percentage of
total species (%)		 属
Genus		 种数
Number of
species		 占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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