生物学杂志

生物学杂志 ›› 2026, Vol. 43 ›› Issue (5): 43-.doi: 10.3969/j.issn.2095-1736.2026.05.043

• 研究报告 • 上一篇    下一篇

乳酸肠球菌FSUH-1中γ-氨基丁酸合成关键基因gadA及gadC的结构与功能分析

聂蔓茹1,2， 李连娇1,2， 郑剑玮1,2， 叶曼诗1,2， 钟先锋2,3， 黄桂东1,2   

  1. 1. 佛山大学 食品科学与工程学院， 佛山 528225； 2. 广东省传统发酵食品工程技术研究中心
    广东省食品流通安全控制工程技术研究中心 佛山市酿造工程技术研究中心 佛山市农业生物
    制造工程技术研究中心， 佛山 528225； 3. 佛山大学 农业与生物工程学院， 佛山 528225
  • 出版日期:2026-10-18 发布日期:2026-10-20
  • 通讯作者: 黄桂东，博士，研究员，研究方向为食品微生物，E-mail：guidongh78@126.com
  • 作者简介:聂蔓茹，硕士研究生，研究方向为食品微生物，E-mail：657164072@qq.com
  • 基金资助:
    国家自然科学基金项目（32372284）； 广东省乡村振兴战略专项种业振兴行动项目（2023WPY00002）； 广东省自然科学基金项目（2021B1515120042， 2023A1515012536）； 广东省乡村振兴战略专项种业振兴行动与科技兴农项目（2024CXTD04）

Structural and functional analysis of the key genes gadA and gadC involved in γ-aminobutyric acid synthesis in Enterococcus lactis FSUH-1

NIE Manru1,2, LI Lianjiao1,2, ZHENG Jianwei1,2, YE Manshi1,2,ZHONG Xianfeng2,3, HUANG Guidong1,2   

  1. 1. School of Food Science and Engineering, Foshan University, Foshan 528225, China; 2. Guangdong Engineering
    Research Center for Traditional Fermented Food, Guangdong Engineering Research Center for Safety Control of Food
    Circulation, Foshan Engineering Research Center for Brewing Technology, Foshan Engineering Research Center for
    Agricultural Biomanufacturing, Foshan 528225, China; 3. School of Agricultural and Biological Engineering,
    Foshan University, Foshan 528225, China
  • Online:2026-10-18 Published:2026-10-20

PDF (PC)

1

摘要： 本文以乳酸肠球菌FSUH-1为研究对象，探讨其γ-氨基丁酸（GABA）合成系统的相关特征。结果表明，FSUH-1具有产谷氨酸脱羧酶（GAD）能力；通过扩增该菌GAD中潜在的关键功能基因，验证了FSUH-1含有乳酸菌合成GABA的关键基因gadA和gadC。采用生物信息学手段，分析预测该菌gadA和gadC这两个基因所编码蛋白结构及功能，发现GadA蛋白为亲水蛋白，不存在跨膜区，无信号肽，为胞内蛋白，是GAD（TIGR01788）结构，具有催化谷氨酸生成GABA的功能；GadC蛋白为疏水蛋白，存在跨膜区，无信号肽，为跨膜蛋白，是GadC（TIGR00910）结构，可介导物质运输及信号转导等功能；将GadA和GadC蛋白三级结构分别与大肠杆菌、乳杆菌CGMCC 1306的蛋白结构进行重叠建模、特征分析，其三级结构核心区域一致，说明该菌的GadA和GadC蛋白保守性高，能介导催化GABA的合成，可为后期定向改造、优化该菌株GABA产量提供新思路。

关键词: 乳酸肠球菌, 谷氨酸脱羧酶, γ-氨基丁酸, 生物信息学分析

Abstract: This study focused onEnterococcus lactisFSUH-1 to investigate the characteristics of its γ-aminobutyric acid （GABA） synthesis system. It demonstrated that FSUH-1 possessed the ability to produce glutamate decarboxylase （GAD）. Potential key functional genes in its genome were amplified, and were verified that FSUH-1 contained the key genesgadAandgadC, which were essential for GABA synthesis in lactic acid bacteria. Bioinformatics methods were employed to analyze and predict the structure and function of the proteins encoded bygadAandgadC. It was found that the GadA protein was a hydrophilic protein without transmembrane regions or a signal peptide, indicating that it was an intracellular protein. It contained the GAD （TIGR01788） domain and was confirmed to catalyze the production of GABA from glutamate. The GadC protein was identified as a hydrophobic protein with transmembrane regions but no signal peptide, and was classified as a transmembrane protein. It contained the GadC （TIGR00910） domain and was predicted to mediate functions such as substrate transport and signal transduction. The tertiary structures of the GadA and GadC proteins were superimposed on and compared with the corresponding protein structures fromEscherichia coliandLactobacillusCGMCC 1306. Results showed that the core regions of their tertiary structures were consistent, indicating that the GadA and GadC proteins in this strain were highly conserved and could mediate the catalytic synthesis of GABA.

Key words: Enterococcus lactis, glutamate decarboxylase, γ-aminobutyric acid, bioinformatics analysis

中图分类号: