Propionate inactivation of butane monooxygenase activity in 'Pseudomonas butanovora': biochemical and physiological implications.
Propionate inactivation of butane monooxygenase activity in 'Pseudomonas butanovora': biochemical and physiological implications.
复制标题
“丁酸假单胞菌”中丁烷单加氧酶活性的丙酸灭活：生化和生理学影响。
DOI：
10.1099/mic.0.2007/008441-0
复制
发表时间：
2007
期刊：
影响因子：
--
通讯作者：
Bottomley,PJ
中科院分区：
文献类型：
--
作者：
Doughty,DM;Halsey,KH;Vieville,CJ;Sayavedra-Soto,LA;Arp,DJ;Bottomley,PJ
丁烷单加氧酶（BMO）在烷烃利用细菌“噬丁烷假单胞菌”中催化烷烃氧化成醇。培养的烷烃生长的'P. butanovora'与丁酸盐或丙酸盐导致不可逆的时间和O2依赖性的BMO活性的损失。相反，BMO活性不受乳酸盐或乙酸盐孵育的影响。氯霉素抑制新的BMO的合成，但没有改变丙酸盐依赖的BMO失活的动力学，这表明丙酸盐的作用不仅仅是由于它作为BMO转录的阻遏物。BMO的保护丙酸依赖性失活的存在下，其天然底物，丁烷。虽然BMO的丙酸盐失活的时间和O2依赖性都意味着丙酸盐可能是自杀底物，但没有证据表明BMO依赖的丙酸盐消耗，或在失活期间由[2- 14 C]丙酸盐对BMO多肽进行14 C标记。还在BMO羟化酶α-亚基中含有单个氨基酸取代的'P. butanovora'突变株中探索了丙酸盐依赖性BMO失活。丙酸依赖性BMO失活在两个突变株的氨基酸取代接近的催化位点不同于野生型（一个是更敏感，另一个少），提供了进一步的证据表明，丙酸依赖性失活涉及与BMO催化位点的相互作用。一个假定的模型，可能会解释丙酸依赖性失活的BMO框架内的催化循环的密切相关的酶，可溶性甲烷单加氧酶的上下文中。
Butane monooxygenase (BMO) catalyses the oxidation of alkanes to alcohols in the alkane-utilizing bacterium ‘Pseudomonas butanovora’. Incubation of alkane-grown ‘P. butanovora’ with butyrate or propionate led to irreversible time- and O2-dependent loss of BMO activity. In contrast, BMO activity was unaffected by incubation with lactate or acetate. Chloramphenicol inhibited the synthesis of new BMO, but did not change the kinetics of propionate-dependent BMO inactivation, suggesting that the propionate effect was not simply due to it acting as a repressor of BMO transcription. BMO was protected from propionate-dependent inactivation by the presence of its natural substrate, butane. Although both the time and O2 dependency of propionate inactivation of BMO imply that propionate might be a suicide substrate, no evidence was obtained for BMO-dependent propionate consumption, or 14C labelling of BMO polypeptides by [2-14C]propionate during inactivation. Propionate-dependent BMO inactivation was also explored in mutant strains of ‘P. butanovora’ containing single amino acid substitutions in the α-subunit of the BMO hydroxylase. Propionate-dependent BMO inactivation in two mutant strains with amino acid substitutions close to the catalytic site differed from wild-type (one was more sensitive and the other less), providing further evidence that propionate-dependent inactivation involves interaction with the BMO catalytic site. A putative model is presented that might explain propionate-dependent inactivation of BMO when framed within the context of the catalytic cycle of the closely related enzyme, soluble methane monooxygenase.
登录
查看更多内容
影响因子：
2.8
作者：
Arp, DJ
通讯作者：
Arp, DJ
DOI：
10.1016/s0021-9258(20)80579-1
发表时间：
1993-10
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Sang-Kyu Lee;J. C. Nesheim;J. D. Lipscomb
通讯作者：
Sang-Kyu Lee;J. C. Nesheim;J. D. Lipscomb
叠氮化物和乙酸盐复合物加上二铁酶 α9 硬脂酰酰基载体蛋白去饱和酶的两种贫铁晶体结构
影响因子：
4.8
作者：
M. Moche;J. Shanklin;A. Ghoshal;Y. Lindqvist
通讯作者：
Y. Lindqvist
影响因子：
2.8
作者：
Dubbels, Bradley L.;Sayavedra-Soto, Luis A.;Arp, Daniel J.
通讯作者：
Arp, Daniel J.
蓖麻 Δ9-18:0-去饱和酶中的单个突变改变了从去饱和到氧化酶化学的反应分配
DOI：
10.1073/pnas.0607165103
发表时间：
2006
期刊：
Proceedings of the National Academy of Sciences
影响因子：
--
作者：
J. Guy;I. A. Abreu;M. Moche;Y. Lindqvist;E. Whittle;J. Shanklin
通讯作者：
J. Shanklin