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微生物低温酶适冷机制研究进展 被引量:12

Progress of Molecular Adaptation of Cold Enzymes from Microorganisms
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摘要 地球寒冷生境中生存着大量微生物。它们必须在酶学水平上对低温导致的生理、生化变化进行调整 ,才能在极端环境中维持生命活力。低温导致化学反应速率下降 ,而低温酶可通过高周转率 (κcat)、高催化效率 (κcat Km)来弥补这种影响。低温酶的一些共性 ,包括低温条件 ( 0~30℃ )下催化活力较高、最适作用温度低、稳定性差以及活化能较低等 ,都可能与蛋白结构的高度柔顺性有关。与高温酶、中温酶相比 ,低温酶中涉及蛋白稳定性的结构因素以及弱相互作用 ,数量减少或发生改变。低温酶可能通过分子内相互作用的减弱、酶分子与溶剂间相互作用的增强 ,并经过适当的构象折叠 。 Numerous microorganisms have been found to have successfully colonized in cold environments of our planet.At the enzyme level,such microorganisms have to cope with the physiological and biochemical changes induced by low temperatures in order to maintain adequate metabolic fluxes.Cold enzymes compensate for the reduction of chemical reaction rates inherent to low temperatures by their high turnover number ( κ cat ) and catalytic efficiency ( κ cat / K m).General characters in common of cold enzymes including higher catalytic activity,lower optimum temperature for enzyme activity,lower stability and lower activation energy at low temperatures of 0~30℃,possibly originate from an increased flexibility of either a selected area of or the overall protein structure.Structural factor and weak interactions involved in protein stability are either reduced in number or modified in order to increase their flexibility when compared to mesophilic or thermophilic homologues.The molecular changes of cold enzymes tend to increase the flexibility of protein structure by a weakening of the intramolecular interactions and by an increase of the interactions with the solvent followed by appropriate folding process of protein conformation.
机构地区 中国极地研究所
出处 《中国生物工程杂志》 CAS CSCD 2003年第10期52-56,共5页 China Biotechnology
基金 国家自然科学基金资助项目 (3 0 2 0 0 0 1 40 0 0 60 10 ) 科技部社会公益研究专项资助项目(2 0 0 1DIA5 0 0 40 -6) 国家海洋局资助项目
关键词 低温酶 分子适应 柔顺性 微生物 适冷机制 Cold enzyme Molecular adaptation Flexibility
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  • 1Zecchinon L, Claverie P, Collins T, et al. Did psychrophilic enzymes really win the challenge? Extremophiles,2001,5: 313 -- 321.
  • 2Irwin JA, Gudmundsson HM, Marteinsson VT, et al. Characterization of alanine and malate dehydrogenases from a marine psychrophile strain PA-43. Extremophiles ,2001,5 : 199 -- 211.
  • 3Galkin A, Kulakova L, Ashida H, et al. Cold-adapted alanine dehydrogenases from two antarctic bacterial strains : Gene cloning,protein characterization, and comparison with mesophilic and thermophilic counterparts. Appl Environ Microbiol, 1999,65 : 4014-- 4020.
  • 4Kulakova L, Galkin A, Kurihara T, et al. Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain Ac10: Gene cloning and enzyme purification and characterization.Appl Environ Microbiol, 1999,65 : 611 -- 617.
  • 5Berchet V, Boulanger D, Gounot AM. Use of gel electrophoresis for the study of enzymatic activities of cold-adapted bacteria. J Microbiol Methods,2000,40:105 -- 110.
  • 6Kristjánsson MM, Magnusson OT, Gudmundsson HM, et al.Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species: Comparison with proteinase K and aqualysin I. Eur J Biochem, 1999,260:752 -- 760.
  • 7Feller G, Arpigny JL, Narinx E, et al. Molecular adaptation of enzymes from psychrophilic organisms. Comp Biochem Physiol,1997, 118A: 495 -- 499.
  • 8Cavicchioli R, Siddiqui KS, Andrews D, et al. Low-temperature extremophiles and their applications. Current Opinion in Biotechnology, 2002,13 : 253 -- 261.
  • 9Kim SY, Hwang KY, Kim SH, et al. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J Biol Chem, 1999,274:11761 -- 11767.
  • 10Feller G, Payan F, Theys F, et al. Stability and structural analysis of a-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem, 1994,222:441 -- 447.

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