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肽脱甲酰化酶及其抑制剂研究进展 被引量：1

Current status of peptide deformylase and its inhibitors
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摘要 肽脱甲酰化酶是细菌生长过程中蛋白质合成所必需的,但在哺乳动物中并不需要,所以肽脱甲酰化酶已成为令人感兴趣的新的抗菌药物作用靶点。肽脱甲酰化酶抑制剂具有广谱抗菌活性和很好的选择性。现综述了近年来相关文献,介绍肽脱甲酰化酶的性质、功能、晶体结构及其抑制剂构效关系的研究进展。 Peptide deformylase(PDF)is an essential enzyme that involves in protein synthesis of bacteria, and is one of the most impressive targets leading to the development of a new generation of broad spectrum and selective antibiotics. This review summarizes the characteristics, crystal structure and function of peptide deformylase in bacteria. Moreover,the structure-activity relationship of PDF inhibitors is discussed.
作者 张大同 贾炯 冯勇 王建武 徐为人 汤立达
机构地区 山东大学化学与化工学院 天津药物研究院
出处 《中国新药杂志》 CAS CSCD 北大核心 2005年第5期530-534,共5页 Chinese Journal of New Drugs
基金 国家重大基础研究前期研究专项(2003CCA027)
关键词 肽脱甲酰化酶 抑制剂 构效关系 peptide deformylase inhibitors structure-activity relationship
分类号 R978.1 [医药卫生—药品] R91 [医药卫生—药学]
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参考文献34

  • 1(a)Adams JM. On the release of the formyl group from nascent protein [ J ]. J Mol Biol, 1968,33 : 571 - 589. (b) Livingston DM, Leder P. Deformylation and protein synthesis[J ]. Biochemistry, 1969,8( 1 ) :435 - 443.
  • 2Meinnel T, Blanquet S. Evidence that Peptide deformylase and methionyl-tRNA (fMet) formyltransferase are encoded within the same operon in Escherichla coli [J ]. J Bacteriol, 1993,175(23) :7737 - 7740.
  • 3Chan MK, Gong WM, Raiagopalan PTR, et al. Crystal structure of the Escherlchla coli peptide deformylase [ J ]. Biochemistry,1997,36 (45) : 13904 - 13909.
  • 4Rajagopalan PTR, Yu XC, Pei DH. Peptide deformylase: a new type of mononuclear iron protein[J]. J Am Chem Soc, 1997,119(150) :12418- 12419.
  • 5Groche D, Becker A, Schlichting l, et al. Isolation and crystallization of functionally competent E. coli peptide deformylase forms containing either iron or nickel in the active site [ J ]. Biochem Biophys Res Commun, 1998,246(2) : 342 - 346.
  • 6Ragusa S, Mouchet P, Lazennec C, et al. Substrate recognition and selectivity of peptide deformylase: Similarities and differences with metzincins and thmolysin[J]. J Mol 13iol, 1999,289 : 1445 - 1457.
  • 7Rajagopalan PT, Grimme S, Pei D. Characterization of cobalt(Ⅱ)-substituted peptide deformylase: Function of the metal ion and the catalytic residue Glu-133 [J ]. Biochemistry, 2000, 39(4):779-790.
  • 8Adams JM, Capecchi MR. N-formylmethionyl-sRNA as the initiator of protein synthesis[J]. Proc Nail Acad Sci USA, 1966,55(1) :147- 155.
  • 9Meinnel T. Methionine as translation start signal:a review of the enzymes of the pathway in Escherichia coli [ J ]. Biochimie ,1993,75(12) : 1061 - 1075.
  • 10Yoshida A, Lin M. NHz-terminal formylmethionine and NH2-terminal methionine cleaving enzymes in rabbits [ J ]. J Biol Chem, 1972,247(3) :952 - 957.

同被引文献8

  • 1FERBER D.Infectious disease:New weapons in the battle of the bugs [ J ].Science,2002,295 (5554):433-434.
  • 2LEVIN BR.Noninherited resistance to antibiotics [ J].Science,2004,305 (5690):1578-1579.
  • 3CALI P,NAERUM L,MUKHIJA S,et al.Isoxazole-3-hydroxamic acid derivatives as peptide deformylase inhibitors aud potential antibacterial agents [ J ].Bioor Med Chem Lett,2004,14 (24):5997-6000.
  • 4RAJAGOPALAN P,YU X,PEI D.Peptide Deformylase:A new type of mononuclear iron protein[ J].J Am Chem Soc,1997,119(50):12418-12419.
  • 5YUAN Z,TRIAS J,WHITE R.Deformylase as a novel antibacterial target[J].Drug Discov Today,2001,6(18):954-961.
  • 6GIGLIONE C,PIERRE M,MEINNEL T.Peptide deformylase as a target for new generation,broad spectrum antimicrobial agents[ J].Mol Microbiol,2001,36:1197-1205.
  • 7CHEN D,PATEL D,WANG C,et al.Actinonin,a naturally occurring antibacterial agent,is a potent deformylase inhibitor[J].Biochemistry,2000,39(6):1256-1262.
  • 8ROBLIN P,HAMMERSCHLAG M.In vitro activity of a new antibiotic NVP-PDF386 (VRC4887) against Chlamydia pneumoniae [ J ].Antimicrob Agents Chemother,2003,47 (4):1447-1448.

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中国新药杂志
2005年 第5期

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