TITLE

Biochemistry: Enzyme's black box cracked open

AUTHOR(S)
Sherman, David H.
PUB. DATE
October 2009
SOURCE
Nature;10/22/2009, Vol. 461 Issue 7267, p1068
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The article focuses on the functionality of polyketide synthase (PKS) enzymes as the biosynthetic machinery that make the molecule to determine the biological activities of polyketides along with other enzymes that adjust polyketide structures to provide additional chemical diversity. It mentions that some of the most confusing and mysterious PKS enzymes are the fungal non-reducing, multi-domain iterative PKSs (NR IPKSs) which convert linear polyketide fragments into polycycles, a series of connected aromatic rings. It notes the mechanism of the product-template (PT) domain, a region of PksA enzyme, which may be expected to be similar to that of fatty acid synthase (FAS) in catalysing polyketide ring-closing reactions.
ACCESSION #
44733475

 

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