生物技术通报 ›› 2013, Vol. 0 ›› Issue (12): 27-35.
赵冉冉, 冯利伟, 张金秀, 徐书景, 鞠建松
收稿日期:
2013-06-04
出版日期:
2013-12-20
发布日期:
2013-12-20
作者简介:
赵冉冉,女,硕士研究生,研究方向:分子酶学;E-mail:867330310@qq.com
基金资助:
Zhao Ranran, Feng Liwei, Zhang Jinxiu, Xu Shujing, Ju Jiansong
Received:
2013-06-04
Published:
2013-12-20
Online:
2013-12-20
摘要: D-氨基酸氧化酶氧化D-氨 基酸生成相应的α-酮 酸和氨,还原型黄素被氧化生成过氧化氢。D-氨基酸氧化酶在精神分裂症的病理、生理学研究和D-氨基酸检测等方面都发挥着关键的作用。主要就结构已解析的几个D-氨基酸氧化酶的序列同源性、结构组成、活性中心、抑制剂以及与辅酶FAD结合能力等方面进行介绍。
赵冉冉, 冯利伟, 张金秀, 徐书景, 鞠建松. D-氨基酸氧化酶结构的研究进展[J]. 生物技术通报, 2013, 0(12): 27-35.
Zhao Ranran, Feng Liwei, Zhang Jinxiu, Xu Shujing, Ju Jiansong. Research Progress on the Crystal Structure of D-amino Acid Oxidase[J]. Biotechnology Bulletin, 2013, 0(12): 27-35.
[1] Sacchi S, Caldinelli L, Cappelletti P, et al. Structure-function relationships in human D-amino acid oxidase[J]. Amino Acids, 2012, 43(5):1833-1850. [2] Conlon HD, Baqai J, Baker K, et al. Two-step immobilized enzyme conversion of cephalosporin C to 7-aminocephalosporanic acid[J]. Biotechnology and Bioengineering, 1995, 46(6):510-513. [3] Berg CP, Rodden FA. Purification of D-amino oxidase from Trigonopsis variabilis[J]. Analytical Biochemistry, 1976, 71(1):214-222. [4] Alonso J, Barredo JL, Diez B, et al. D-amino-acid oxidase gene from Rhodotorula gracilis(Rhodosporidium toruloides )ATCC 26217[J]. Microbiology(Reading, England), 1998, 144(Pt 4):1095-1101. [5] Mattevi A, Vanoni MA, Todone F, et al. Crystal structure of D-amino acid oxidase:a case of active site mirror-image convergent evolution with flavocytochrome b2[J]. Proceedings of the National Academy of Sciences of the United States of America, 1996, 93(15):7496-7501. [6] Mizutani H, Miyahara I, Hirotsu K, et al. Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution[J]. Journal of Biochemistry, 1996, 120(1):14-17. [7] Todone F, Vanoni MA, Mozzarelli A, et al. Active site plasticity in D-amino acid oxidase:a crystallographic analysis[J]. Biochemi-stry, 1997, 36(19):5853-5860. [8] Pollegioni L, Diederichs K, Molla G, et al. Yeast D-amino acid oxidase:structural basis of its catalytic properties[J]. Journal of Molecular Biology, 2002, 324(3):535-546. [9] Duplantier AJ, Becker SL, Bohanon MJ, et al. Discovery, SAR, and pharmacokinetics of a novel 3-hydroxyquinolin-2(1H)-one series of potent D-amino acid oxidase(DAAO)inhibitors[J]. Journal of Medicinal Chemistry, 2009, 52(11):3576-3585. [10] Kawazoe T, Tsuge H, Imagawa T, et al. Structural basis of D-DOPA oxidation by D-amino acid oxidase:alternative pathway for dopa-mine biosynthesis[J]. Biochemical and Biophysical Research Communications, 2007, 355(2):385-391. [11] Sparey T, Abeywickrema P, Almond S, et al. The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase(DAO)inhibitors[J]. Bioorganic & Medicinal Chemistry Letters, 2008, 18(11):3386-3391. [12] Kawazoe T, Tsuge H, Pilone MS, Fukui K. Crystal structure of human D-amino acid oxidase:context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring[J]. Protein Science, 2006, 15(12):2708-2717. [13] Holm L, Sander C. Protein structure comparison by alignment of distance matrices[J]. Journal of Molecular Biology, 1993, 233(1):123-138. [14] Pilone Simonetta M, Pollegioni L, Casalin P, et al. Properties of D-amino-acid oxidase from Rhodotorula gracilis[J]. European Journal of Biochemistry / FEBS, 1989, 180(1):199-204. [15] Tarelli GT, Vanoni MA, Negri A, Curti B. Characterization of a fully active N-terminal 37-kDa polypeptide obtained by limited tryptic cleavage of pig kidney D-amino acid oxidase[J]. The Journal of Biological Chemistry, 1990, 265(34):21242-21246. [16] Pollegioni L, Piubelli L, Sacchi S, et al. Physiological functions of D-amino acid oxidases:from yeast to humans[J]. Cellular and Molecular Life Sciences:CMLS, 2007, 64(11):1373-1394. [17] Molla G, Sacchi S, Bernasconi M, et al. Characterization of human D-amino acid oxidase[J]. FEBS Letters, 2006, 580(9):2358-2364. [18] Caldinelli L, Iametti S, Barbiroli A, et al. Unfolding intermediate in the peroxisomal flavoprotein D-amino acid oxidase[J]. The Journal of Biological Chemistry, 2004, 279(27):28426-28434. [19] Caldinelli L, Molla G, Pilone MS, Pollegioni L. Tryptophan 243 affects interprotein contacts, cofactor binding and stability in D-amino acid oxidase from Rhodotorula gracilis [J]. The FEBS Journal, 2006, 273(3):504-512. [20] Pilone MS. D-Amino acid oxidase:new findings[J]. Cell Mol Life Sci:CMLS, 2000, 57(12):1732-1747. [21] Piubelli L, Caldinelli L, Molla G, et al. Conversion of the dimeric D-amino acid oxidase from Rhodotorula gracilis to a monomeric form. A rational mutagenesis approach[J]. FEBS Letters, 2002, 526(1-3):43-48. [22] Piubelli L, Molla G, Caldinelli L, et al. Dissection of the structural determinants involved in formation of the dimeric form of D-amino acid oxidase from Rhodotorula gracilis :role of the size of the betaF5-betaF6 loop[J]. Protein Engineering, 2003, 16(12):1063-1069. [23] Pollegioni L, Iametti S, Fessas D, et al. Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase[J]. Protein Science, 2003, 12(5):1018-1029. [24] Boselli A, Piubelli L, Molla G, et al. On the mechanism of Rhodotorula gracilis D-amino acid oxidase:role of the active site serine 335[J]. Biochimica et Biophysica Acta, 2004, 1702(1):19-32. [25] Miura R, Setoyama C, Nishina Y, et al. Porcine kidney d-amino acid oxidase:the three-dimensional structure and its catalytic mechanism based on the enzyme-substrate complex model[J]. Journal of Molecular Catalysis B:Enzymatic, 2001, 12(1):43-52. [26] Pollegioni L, Fukui K, Massey V. Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228[J]. The Journal of Biological Chemistry, 1994, 269(50):31666-31673. [27] Harris CM, Molla G, Pilone MS, Pollegioni L. Studies on the reaction mechanism of Rhodotorula gracilis D-amino-acid oxidase. Role of the highly conserved Tyr-223 on substrate binding and catalysis[J]. The Journal of Biological Chemistry, 1999, 274(51):36233-36240. [28] Molla G, Porrini D, Job V, et al. Role of arginine 285 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study[J]. The Journal of Biological Chemistry, 2000, 275(32):24715-24721. [29] Boselli A, Sacchi S, Job V, et al. Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study[J]. European Journal of Biochemistry / FEBS, 2002, 269(19):4762-4771. [30] Pollegioni L, Sacchi S, Caldinelli L, et al. Engineering the properties of D-amino acid oxidases by a rational and a directed evolution approach[J]. Curr Protein Pept Sci, 2007, 8(6):600-618. [31] Sarower MG, Okada S, Abe H. Catalytic and structural characteri-stics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia coli. [J].Comp Biochem Physiol B Biochem Mol Biol, 2005, 140(3):417-425. [32] Caldinelli L, Molla G, Sacchi S, et al. Relevance of weak flavin binding in human D-amino acid oxidase[J]. Protein Science, 2009, 18(4):801-810. [33] Sacchi S, Caldinelli L, Cappelletti P, et al. Structure-function relationships in human D:-amino acid oxidase[J]. Amino Acids, 2012. [34] Kawazoe T, Park HK, Iwana S, et al. Human D-amino acid oxidase:an update and review[J]. Chem Rec, 2007, 7(5):305-315. [35] Geueke B, Weckbecker A, Hummel W. Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae [J]. Applied Microbiology and Biotechnology, 2007, 74(6):1240-1247. [36] Lin L, Chien HR, Wang W, et al. Expression of Trigonopsis variabilis D-amino acid oxidase gene in Escherichia coli and characterization of its inactive mutants[J]. Enzyme and Microbial Technology, 2000, 27(7):482-491. [37] Gao J, Kelly JW. Toward quantification of protein backbone-backbone hydrogen bonding energies:An energetic analysis of an amide-to-ester mutation in an alpha-helix within a protein[J]. Protein Science, 2008, 17(6):1096-1101. [38] Porter DJ, Voet JG, Bright HJ. Mechanistic features of the D-amino acid oxidase reaction studied by double stopped flow spectrophotometry[J]. The Journal of Biological Chemistry, 1977, 252(13):4464-4473. [39] Klein JR. Inhibition of D-amino acid oxidase by aromatic acids[J]. The Journal of Biological Chemistry, 1953, 205(2):725-730. [40] Ferraris DV, Tsukamoto T. Recent advances in the discovery of D-amino acid oxidase inhibitors and their therapeutic utility in schizophrenia[J]. Current Pharmaceutical Design, 2011, 17(2):103-111. [41] Pollegioni L, Caldinelli L, Molla G, et al. Catalytic properties of D-amino acid oxidase in cephalosporin C bioconversion:a comparison between proteins from different sources[J]. Biotechnology Progress, 2004, 20(2):467-473. [42] Umhau S, Pollegioni L, Molla G, et al. The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation[J]. Proc Natl Acad Sci US A, 2000, 97(23):12463-12468. [43] Subramani S. Protein import into peroxisomes and biogenesis of the organelle[J]. Annu Rev Cell Biol, 1993, 9:445-478. [44] Sacchi S, Rosini E, Pollegioni L, Molla G. D-amino acid oxidase inhibitors as a novel class of drugs for schizophrenia therapy[J]. Current Pharmaceutical Design, 2013, 19(14):2499-2511. [45] Lu JM, Gong N, Wang YC, Wang YX. D-Amino acid oxidase-mediated increase in spinal hydrogen peroxide is mainly responsible for formalin-induced tonic pain[J]. British Journal of Pharmacology, 2012, 165(6):1941-1955. [46] Zhao WJ, Gao ZY, Wei H, et al. Spinal D-amino acid oxidase cont- ributes to neuropathic pain in rats[J]. The Journal of Pharmacol-ogy and Experimental Therapeutics, 2010, 332(1):248-254. [47] Hou YC, Lai CH. A kind of d-amino Acid oxidase inhibitor, sodium benzoate, might relieve panic symptoms in a first-episode, drug-naive panic-disorder patient[J]. The Journal of Neuropsychiatry and Clinical Neurosciences, 2013, 25(2):E07-08. [48] Lai CH. Sodium benzoate, a D-amino acid oxidase inhibitor, increased volumes of thalamus, amygdala, and brainstem in a drug-naive patient with major depression[J]. The Journal of Neuropsychiatry and Clinical Neurosciences, 2013, 25(1):E50-51. [49] Raje M, Hin N, Duvall B, et al. Synthesis of kojic acid derivatives as secondary binding site probes of d-amino acid oxidase[J]. Bioorg Med Chem Lett, 2013, 23(13):3910-3913. [50] Caligiuri A, D'Arrigo P, Rosini E, et al. Activity of yeast d-amino acid oxidase on aromatic unnatural amino acids[J]. Journal of Molecular Catalysis B:Enzymatic, 2008, 50(2-4):93-98. [51] Mueller M, Kratzer R, Schiller M, et al. The role of Cys108 in Trigonopsis variabilis d-amino acid oxidase examined through chemical oxidation studies and point mutations C108S and C108D[J]. Biochimica et Biophysica Acta, 2010, 1804(7):1483-1491. [52] Wong KS, Fong WP, Tsang PW. A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilis D-amino acid oxidase[J]. N Biotechnol, 2010, 27(1):78-84. [53] Komarova NV, Golubev IV, Khoronenkova SV, et al. Engineering of substrate specificity of D-Amino acid oxidase from the yeast Trigonopsis variabilis :directed mutagenesis of Phe258 residue[J]. Biochemistry, 2012, 77(10):1181-1189. |
[1] | 董聪, 高庆华, 王玥, 罗同阳, 王庆庆. 基于联合策略提高FAD依赖的葡萄糖脱氢酶的酵母表达[J]. 生物技术通报, 2023, 39(6): 316-324. |
[2] | 刘艺云, 邓利敏, 岳慧颖, 岳超, 刘健华. 质粒接合转移及其抑制剂的研究进展[J]. 生物技术通报, 2022, 38(9): 35-46. |
[3] | 代文双, 刘会云, 杜庆国, 邹枨, 王轲. 组蛋白去乙酰化酶抑制剂(HDACi)对小麦基因编辑效率的影响及转录组学分析[J]. 生物技术通报, 2021, 37(1): 2-14. |
[4] | 江芮, 吕柯孬, 潘学峰, 崔新霞, 申世刚, 丁良. 表观遗传药物研发的现状与挑战[J]. 生物技术通报, 2019, 35(8): 213-225. |
[5] | 董聪, 高庆华, 王玥, 罗同阳. 基于密码子优化的FAD依赖葡萄糖脱氢酶在毕赤酵母中的高效表达及酶学性质[J]. 生物技术通报, 2019, 35(7): 114-120. |
[6] | 黄湘湄, 吴雅茜, 刘颖, 梁嘉烨, 苏伟明. 海洋源乳酸菌AI-2类群体感应抑制剂对单增李斯特菌抑制效果研究[J]. 生物技术通报, 2019, 35(4): 36-42. |
[7] | 乔晶, 崔晟榕, 石宏武, 罗祖良, 马小军. 罗汉果环阿屯醇合酶的同源建模、分子对接及催化环化的机理推测[J]. 生物技术通报, 2019, 35(2): 101-108. |
[8] | 林贝, 李健秀, 刘雪凌. 木质纤维素水解副产物对乙醇发酵的影响及应对措施[J]. 生物技术通报, 2018, 34(3): 23-30. |
[9] | 程杏安, 叶静敏, 蒋旭红, 刘展眉, 胡美英. 草地贪夜蛾组织蛋白酶B的基因克隆、序列分析、三维结构预测及其分子对接模拟[J]. 生物技术通报, 2018, 34(1): 183-194. |
[10] | 龙翔宇, 梁启福, 戚继艳, 方永军, 唐朝荣. 橡胶树半胱氨酸蛋白酶抑制剂HbCYS2的克隆与表达分析[J]. 生物技术通报, 2017, 33(3): 86-92. |
[11] | 刘秀侠, 徐海燕, 辛国芹, 穆熙军, 孙学森, 谷巍. 一株枯草芽孢杆菌噬菌体的生物学特性分析及抗性菌株的诱变筛选[J]. 生物技术通报, 2017, 33(2): 143-148. |
[12] | 刘贺, 朱家庆, 纵秋瑾, 李炳志, 元英进. 生物质转化工程酿酒酵母的研究进展[J]. 生物技术通报, 2017, 33(1): 93-98. |
[13] | 张晶, 孙瑞秋, 唐延婷, 刘祥. 以MIF为靶标的抑制剂药物高通量筛选模型的建立和应用[J]. 生物技术通报, 2016, 32(9): 253-259. |
[14] | 李远,黄洁琼,李佳俊,汪维鹏,张洪建. CYP2C8及CYP3A4细胞表达体系的构建及其在小分子激酶药物对紫衫醇代谢途径抑制研究中的应用[J]. 生物技术通报, 2016, 32(7): 227-233. |
[15] | 龙玲, 杨艳, 朱乃硕. 应用比色法检测枯草芽孢杆菌变异菌株中1-脱氧野尻霉素含量[J]. 生物技术通报, 2016, 32(6): 187-192. |
阅读次数 | ||||||
全文 |
|
|||||
摘要 |
|
|||||