Beyond ethylmalonyl-CoA: the functional role of crotonyl-CoA carboxylase/reductase homologs in expanding polyketide diversity
Covering: up through August 2011 This review covers the emerging biosynthetic role of
crotonyl-CoA carboxylase/reductase (CCR) homologs in extending the structural and
functional diversity of polyketide natural products. CCRs catalyze the reductive carboxylation
of α, β-unsaturated acyl-CoA substrates to produce a variety of substituted malonyl-CoA
derivatives employed as polyketide synthase extender units. Here we discuss the history of
CCRs in both primary and secondary metabolism, the mechanism by which they function …
crotonyl-CoA carboxylase/reductase (CCR) homologs in extending the structural and
functional diversity of polyketide natural products. CCRs catalyze the reductive carboxylation
of α, β-unsaturated acyl-CoA substrates to produce a variety of substituted malonyl-CoA
derivatives employed as polyketide synthase extender units. Here we discuss the history of
CCRs in both primary and secondary metabolism, the mechanism by which they function …
Covering: up through August 2011 This review covers the emerging biosynthetic role of crotonyl-CoA carboxylase/reductase (CCR) homologs in extending the structural and functional diversity of polyketide natural products. CCRs catalyze the reductive carboxylation of α,β-unsaturated acyl-CoA substrates to produce a variety of substituted malonyl-CoA derivatives employed as polyketide synthase extender units. Here we discuss the history of CCRs in both primary and secondary metabolism, the mechanism by which they function, examples of new polyketide diversity from pathway specific CCRs, and the role of CCRs in facilitating the bioengineering novel polyketides.
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