Catalytic role of the C-terminal domains of a fungal non-reducing polyketide synthase

被引:28
作者
Fisch, Katja M. [1 ]
Skellam, Elizabeth [1 ]
Ivison, David [1 ]
Cox, Russell J. [1 ]
Bailey, Andrew M. [2 ]
Lazarus, Colin M. [2 ]
Simpson, Thomas J. [1 ]
机构
[1] Univ Bristol, Sch Chem, Bristol BS8 1TS, Avon, England
[2] Univ Bristol, Sch Biol Sci, Bristol BS8 1UG, Avon, England
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
NIDULANS-WA GENE; ASPERGILLUS-NIDULANS; PENICILLIUM STIPITATUM; BIOSYNTHESIS; TROPOLONES; MECHANISM; ACIDS;
D O I
10.1039/c0cc01162b
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The in vivo activity of truncated forms of methylorcinaldehyde synthase shows that the synthase retains a hydrolytic release activity in the absence of reductive chain release and that chain-length is not controlled by the reductive release domain; experiments using a methyltransferase inhibitor suggest that methylation occurs prior to aromatisation.
引用
收藏
页码:5331 / 5333
页数:3
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