枯草芽孢杆菌
化学
大肠杆菌
生物化学
突变
重组DNA
吡哆醛
体外
磷酸吡哆醛
基因
酶
分子生物学
突变
细菌
生物
遗传学
辅因子
作者
Chinmayi R. Kaundinya,H.S. Savithri,K. Krishnamurthy Rao,Petety V. Balaji
出处
期刊:Glycobiology
[Oxford University Press]
日期:2018-07-27
卷期号:28 (10): 802-812
被引量:9
标识
DOI:10.1093/glycob/cwy063
摘要
The gene epsN of Bacillus subtilis 168 was cloned and overexpressed in Escherichia coli. Purified recombinant EpsN is shown to be a pyridoxal 5'-phosphate (PLP)-dependent aminotransferase by absorption spectroscopy, l-cycloserine inhibition and reverse phase HPLC studies. EpsN catalyzes the conversion of UDP-2,6-dideoxy 2-acetamido 4-keto glucose to UDP-2,6-dideoxy 2-acetamido 4-amino glucose. Lys190 was found by sequence comparison and site-directed mutagenesis to form Schiff base with PLP. Mutagenesis studies showed that, in addition to Lys190, Ser185, Glu164, Gly58 and Thr59 are essential for aminotransferase activity.
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