[1] 周大祥, 龙泉洲, 殷幼平, 等. 青枯雷尔氏菌Ⅲ型分泌系统hrcN基因的功能分析[J]. 中国生物防治学报, 2021, 37 (6):1353-1362. [2] Wei Z, Huang J F, Hu J, et al. Altering transplantation time to avoid periods of high temperature can efficiently reduce bacterial wilt disease incidence with tomato[J]. PLoS ONE, 2015, 10(10):e0139313. [3] Jacobs J M, Babujee L, Meng F, et al. The in planta transcriptome of Ralstonia solanacearum:conserved physiological and virulence strategies during bacterial wilt of tomato[J]. mBio, 2012, 3(4):e00114-12. [4] Zhou D X, Li GL, Sun H L, et al. In silico studies reveal RSc1154 and RhlE as temperature-related pathogenic proteins of Ralstonia solanacearum[J]. FEMS Microbiology Letters, 2019, 366(15):1-8. [5] Yum D Y, Lee B Y, Pan J G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli[J]. Applied and Environmental Microbiology, 1999, 65(8):3341-3346. [6] Habrych M, Rodriguez S, Stewart J D. Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE[J]. Biotechnology Progress, 2002, 18(2):257-261. [7] Thornalley P J, Langborg A, Minhas H S. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose[J]. Biochemical Journal, 1999, 344(1):109-116. [8] Rondeau P, Bourdon E. The glycation of albumin:Structural and functional impacts[J]. Biochimie, 2011, 93(4):645-658. [9] Ko J, Kim I, Yoo S et al. Conversion of methylglyoxal to acetol by Escherichia coli aldo-Keto reductases[J]. Journal of Microbiology, 2005,187(16):5782-5789. [10] Lee C, Kim I, Park C. Glyoxal detoxification in Escherichia coli K-12 by NADPH dependent aldo-keto reductases[J]. Journal of Microbiology, 2013, 51(4):527-530. [11] Khurana S, Powers D B, Anderson S, et al. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution[J]. Proceedings of the National Academy of Sciences of the United States of America, 1998, 95(12):6768-6773. [12] Khurana S, Sanli G, Powers D B, et al. Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases[J]. Proteins Structure Function and Bioinformatics, 2000, 39(1):68-75. [13] Zelić B, Pavlović N, Delić V, et al. Optimization of pH and temperature in the process of bioconversion of glucose to 2,5-diketo-D-gluconic acid[J]. Chemical and Biochemical Engineering Quaterly, 2002, 16(1):7-11. [14] Kaswurm V, Pacher C, Kulbe K D, et al. 2,5-Diketo-gluconic acid reductase from Corynebacterium glutamicum:Characterization of stability, catalytic properties and inhibition mechanism for use in vitamin C synthesis[J]. Process Biochemistry, 2012, 47(1):2012-2019. [15] Togo T. Cell membrane disruption stimulates cAMP and Ca2+signaling to potentiate cell membrane resealing in neighboring cells[J]. Biology Open, 2017, 6(12):1814-1819. [16] He L Y, Sequeira L, Kelman A. Characteristics of strains of Pseudomonas solanacearum[J]. Plant Disease, 1983, 67(2):1357-1361. [17] Meng F, Yao J, Allen C. A MotN mutant of Ralstonia solanacearum is hypermotile and has reduced virulence[J]. Journal of Bacteriology, 2011, 193(10):2477-2486. [18] Miller E N, Jarboe L R, Yomano L P, et al. Silencing of NADPH-dependent oxidoreductase genes (yqhD and dkgA) in furfural-resistant ethanologenic Escherichia coli[J]. Applied and Environmental Microbiology, 2009, 75(13):4315-4323. [19] Chen M, Nan Chen N, Wang J W, et al. Involvement of a FAD-Linked Oxidase RSc0454 for Expression of the Type III Secretion System and Pathogenicity in Ralstonia solanacearum[J]. Molecular Plant-microbe Interactions, 2021, 34(11):1228-1235. [20] Tang M X, Bouchez O, Cruveiller S, et al. Modulation of Quorum Sensing as an Adaptation to Nodule Cell Infection during Experimental Evolution of Legume Symbionts[J]. Mbio, 2020, 11(1):e03129-19. [21] Qi P P, Huang M L, Hu X H, et al. A Ralstonia solanacearum effector targets TGA transcription factors to subvert salicylic acid signaling[J]. The Plant Cell, 2022, 34(5):1666-1683. [22] Gao L L, Hu Y D, Liu J C, et al. Stepwise metabolic engineering of Gluconobacter oxydans WSH-003 for the direct production of 2-keto-L-gulonic acid from D-sorbitol[J]. Metabolic Engineering, 2014, 24(5):30-37. [23] Kaswurm V, Van Hecke W, Kulbe K D, et al. Engineering of a bi-enzymatic reaction for efficient production of the ascorbic acid precursor 2-keto-L-gulonic acid[J]. Biochemical Engineering Journal, 2013(3), 79:104-111. [24] Sanli G, Banta S, Aanderson S, et al. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase[J]. Protein Science, 2004, 13(2):504-512. |