Purification and partial characterization of the Pyrococcus horikoshii methylmalonyl-CoA epimerase.
Purification and partial characterization of the Pyrococcus horikoshii methylmalonyl-CoA epimerase.
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堀越火球菌甲基丙二酰辅酶 A 差向异构酶的纯化和部分表征。
DOI：
10.1007/s00253-003-1474-5
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发表时间：
2004
影响因子：
5
通讯作者：
Rasche,ME
中科院分区：
文献类型：
--
作者：
Bobik,TA;Rasche,ME
Methylmalonyl-CoA epimerase (MCE) from the hyperthermophilic archaeon,Pyrococcus horikoshii, was expressed at high levels inEscherichia coli, purified, and partially characterized. TheP. horikoshiiMCE enzyme was a homodimer with an apparent molecular mass of 31,700 Da. TheKmof the enzyme for methylmalonyl-CoA was 79 μM and thekcatwas 240 s−1. TheP. horikoshiienzyme was extremely heat-stable and withstood boiling for 60 min without detectable loss in activity.
