The structure of SpnF, a standalone enzyme that catalyzes [4+2] cycloaddition

被引:1
|
作者
Fage, Christopher D. [1 ]
Isiorho, Eta A. [1 ]
Liu, Yungnan [2 ]
Wagner, Drew T. [1 ]
Liu, Hung-wen [2 ,3 ]
Keatinge-Clay, Adrian T. [1 ,3 ]
机构
[1] Univ Texas Austin, Dept Mol Biosci, Austin, TX 78712 USA
[2] Univ Texas Austin, Coll Pharm, Div Med Chem, Austin, TX 78712 USA
[3] Univ Texas Austin, Dept Chem, Austin, TX 78712 USA
基金
美国国家卫生研究院;
关键词
MACROPHOMATE SYNTHASE; DIELS-ALDER; BIOSYNTHESIS; CYCLIZATION; EVOLUTION; SPINOSYNS; INSIGHT; CLUSTER;
D O I
10.1038/NCHEMBIO.1768
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the biosynthetic pathway of the spinosyn insecticides, the tailoring enzyme SpnF performs a [4 + 2] cycloaddition on a 22-membered macrolactone to forge an embedded cyclohexene ring. To learn more about this reaction, which could potentially proceed through a Diels-Alder mechanism, we determined the 1.50-angstrom-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.
引用
收藏
页码:256 / +
页数:5
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