Abstract：
:The borrelidin polyketide synthase (PKS) begins with a carboxylated substrate and, unlike typical decarboxylative loading PKSs, retains the carboxy group in the final product. The specificity and tolerance of incorporation of carboxyacyl substrate into type I PKSs have not been explored. Here, we show that the first extension module is promiscuous in its ability to extend both carboxyacyl and non-carboxyacyl substrates. However, the loading module has a requirement for substrates containing a carboxy moiety, which are not decarboxylated in situ. Thus, the loading module is the basis for the observed specific incorporation of carboxylated starter units by the borelidin PKS.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Hagen A,Poust S,de Rond T,Yuzawa S,Katz L,Adams PD,Petzold CJ,Keasling JDdoi
10.1021/bi500951csubject
Has Abstractpub_date
2014-09-30 00:00:00pages
5975-7issue
38eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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