详细信息

OvoAMtht from Methyloversatilis thermotolerans ovothiol biosynthesis is a bifunction enzyme: thiol oxygenase and sulfoxide synthase activities  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:OvoAMtht from Methyloversatilis thermotolerans ovothiol biosynthesis is a bifunction enzyme: thiol oxygenase and sulfoxide synthase activities

作者:Cheng, Ronghai[1];Weitz, Andrew C.[1];Paris, Jared[2];Tang, Yijie[2];Zhang, Jingyu[3];Song, Heng[1];Naowarojna, Nathchar[1];Li, Kelin[1];Qiao, Lu[1];Lopez, Juan[1];Grinstaff, Mark W.[1];Zhang, Lixin[3];Guo, Yisong[2];Elliott, Sean[1];Liu, Pinghua[1]

机构:[1]Boston Univ, Dept Chem, 590 Commonwealth Ave, Boston, MA 02215 USA;[2]Carnegie Mellon Univ, Dept Chem, 4400 Fifth Ave, Pittsburgh, PA 15213 USA;[3]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China

年份:2022

卷号:13

期号:12

起止页码:3589

外文期刊名:CHEMICAL SCIENCE

收录:;EI(收录号:20221311858300);WOS:【SCI-EXPANDED(收录号:WOS:000765892100001)】;

基金:This work is partially supported by the National Science Foundation (CHE-2004109 to P. Liu, CHE-1654060 to Y. Guo) and National Institute of Health (R35-GM136294 to S. Elliott, and GM140040 to P. Liu).

语种:英文

外文关键词:Enzymes - Amino acids - Biochemistry - Electronic properties - Iron - Porphyrins

摘要:Mononuclear non-heme iron enzymes are a large class of enzymes catalyzing a wide-range of reactions. In this work, we report that a non-heme iron enzyme in Methyloversatilis thermotolerans, OvoA(Mtht,) has two different activities, as a thiol oxygenase and a sulfoxide synthase. When cysteine is presented as the only substrate, OvoA(Mtht) is a thiol oxygenase. In the presence of both histidine and cysteine as substrates, OvoA(Mtht) catalyzes the oxidative coupling between histidine and cysteine (a sulfoxide synthase). Additionally, we demonstrate that both substrates and the active site iron's secondary coordination shell residues exert exquisite control over the dual activities of OvoA(Mtht) (sulfoxide synthase vs. thiol oxygenase activities). OvoA(Mtht) is an excellent system for future detailed mechanistic investigation on how metal ligands and secondary coordination shell residues fine-tune the iron-center electronic properties to achieve different reactivities.

参考文献:

正在载入数据...

版权所有©华东理工大学 重庆维普资讯有限公司 渝B2-20050021-7 
渝公网安备 50019002500408号 违法和不良信息举报中心