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首页> 美国卫生研究院文献>Microorganisms >Characterised Flavin-Dependent Two-Component Monooxygenases from the CAM Plasmid of Pseudomonas putida ATCC 17453 (NCIMB 10007): ketolactonases by Another Name
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Characterised Flavin-Dependent Two-Component Monooxygenases from the CAM Plasmid of Pseudomonas putida ATCC 17453 (NCIMB 10007): ketolactonases by Another Name

机译：恶臭假单胞菌ATCC 17453（NCIMB 10007）CAM质粒中表征的黄素依赖性双组分单加氧酶：酮内酯酶的别名

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摘要

The CAM plasmid-coded isoenzymic diketocamphane monooxygenases induced in Pseudomonas putida ATCC 17453 (NCIMB 10007) by growth of the bacterium on the bicyclic monoterpene (rac)-camphor are notable both for their interesting history, and their strategic importance in chemoenzymatic syntheses. Originally named ‘ketolactonase—an enzyme system for cyclic lactonization’ because of its characterised mode of action, (+)-camphor-induced 2,5-diketocamphane 1,2-monooxygenase was the first example of a Baeyer-Villiger monooxygenase activity to be confirmed in vitro. Both this enzyme and the enantiocomplementary (−)-camphor-induced 3,6-diketocamphane 1,6-monooxygenase were mistakenly classified and studied as coenzyme-containing flavoproteins for nearly 40 years before being correctly recognised and reinvestigated as FMN-dependent two-component monooxygenases. As has subsequently become evident, both the nature and number of flavin reductases able to supply the requisite reduced flavin co-substrate for the monooxygenases changes progressively throughout the different phases of camphor-dependent growth. Highly purified preparations of the enantiocomplementary monooxygenases have been exploited successfully for undertaking both nucleophilic and electrophilic biooxidations generating various enantiopure lactones and sulfoxides of value as chiral synthons and auxiliaries, respectively. In this review the chequered history, current functional understanding, and scope and value as biocatalysts of the diketocamphane monooxygenases are discussed.
机译：通过细菌在双环单萜（rac）樟脑上的生长在恶臭假单胞菌ATCC 17453（NCIMB 10007）中诱导的CAM质粒编码的同工酶双酮环戊烷单加氧酶以其有趣的历史和在化学酶促合成中的战略重要性而著称。 （+）-樟脑诱导的2,5-二酮庚烷1,2-单加氧酶由于其独特的作用方式，最初被称为“酮内酯酶-环内酯化的酶系统”，是第一个将Baeyer-Villiger单加氧酶活性的实例。体外证实。此酶和对映体互补（-）-樟脑诱导的3,6-diketocamphane 1,6-单加氧酶被错误地分类为含辅酶的黄素，并将其研究了将近40年，然后才被正确识别并重新研究为FMN依赖的二组分单加氧酶。如随后变得明显的，能够为单加氧酶提供必需的减少的黄素共底物的黄素还原酶的性质和数目在樟脑依赖性生长的不同阶段中逐渐变化。对映体互补单加氧酶的高纯度制剂已被成功地用于亲核和亲电子生物氧化反应，分别产生手性合成子和助剂的各种对映体纯内酯和亚砜。在这篇综述中，讨论了方格历史，当前的功能理解，范围和作为二酮庚烷单加氧酶的生物催化剂的价值。

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