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定点突变 sp.植酸酶 N 端结构域中极性氨基酸残基对酶活性的影响。

Effect of Polar Amino Acid Residue Substitution by Site-Directed Mutagenesis in the N-terminal Domain of sp. Phytase on Enzyme Activity.

机构信息

Department of Biotechnology, Pukyong National University, Busan 48513, Republic of Korea.

出版信息

J Microbiol Biotechnol. 2020 Jul 28;30(7):2003-3020. doi: 10.4014/jmb.2003.03020.

DOI:10.4014/jmb.2003.03020
PMID:32325546
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9728340/
Abstract

The N-terminal domain of the sp. FB15 phytase increases low-temperature activity and catalytic efficiency. In this study, the 3D structure of the N-terminal domain was predicted and substitutions for the amino acid residues of the region assumed to be the active site were made. The activity of mutants, in which alanine (A) was substituted for the original residue, was investigated at various temperatures and pH values. Significant differences in enzymatic activity were observed only in mutant E263A, suggesting that the amino acid residue at position 263 of the N-terminal domain is important in enzyme activity.

摘要

sp. FB15 植酸酶的 N 端结构域提高了低温活性和催化效率。在本研究中，预测了 N 端结构域的三维结构，并对假定为活性位点的区域的氨基酸残基进行了取代。在不同温度和 pH 值下，研究了突变体中丙氨酸（A）取代原始残基的活性。仅在突变体 E263A 中观察到酶活性的显著差异，这表明 N 端结构域第 263 位的氨基酸残基对酶活性很重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/8ef8bd3d5dfb/JMB-30-7-1104-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/0cf55af7c1b4/JMB-30-7-1104-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/954ca7e9f2fb/JMB-30-7-1104-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/9160bb21f71c/JMB-30-7-1104-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/8ef8bd3d5dfb/JMB-30-7-1104-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/0cf55af7c1b4/JMB-30-7-1104-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/954ca7e9f2fb/JMB-30-7-1104-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/9160bb21f71c/JMB-30-7-1104-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/088a/9728340/8ef8bd3d5dfb/JMB-30-7-1104-f4.jpg

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本文引用的文献

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Enzyme Microb Technol. 2019 Jul;126:69-76. doi: 10.1016/j.enzmictec.2019.04.002. Epub 2019 Apr 3.
2
N-terminal domain of the beta-propeller phytase of Pseudomonas sp. FB15 plays a role for retention of low-temperature activity and catalytic efficiency.假单胞菌 FB15 的β-折叠植酸酶的 N 端结构域在保持低温活性和催化效率方面发挥作用。
Enzyme Microb Technol. 2018 Oct;117:84-90. doi: 10.1016/j.enzmictec.2018.06.008. Epub 2018 Jun 19.
3
Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys.
Int J Biol Macromol. 2017 Jan;94(Pt A):594-602. doi: 10.1016/j.ijbiomac.2016.10.043. Epub 2016 Oct 17.
4
Site-directed mutagenesis of an alkaline phytase: influencing specificity, activity and stability in acidic milieu.定点突变碱性植酸酶：影响酸性环境下的特异性、活性和稳定性。
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5
Phytate and phytase in fish nutrition.植物酸盐和植酸酶在鱼类营养中的应用。
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6
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