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Front Cover: Transacylation Kinetics in Fatty Acid and Polyketide Synthases and its Sensitivity to Point Mutations (ChemCatChem 12/2021)
Author(s) -
Stegemann Franziska,
Grininger Martin
Publication year - 2021
Publication title -
chemcatchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.202100731
Subject(s) - polyketide , compartmentalization (fire protection) , acyl carrier protein , substrate (aquarium) , biochemistry , chemistry , enzyme , cofactor , acyltransferases , metabolite , active site , nanopore , stereochemistry , biology , biosynthesis , nanotechnology , materials science , ecology
The Front Cover shows an example of polyketide synthases, producing complex products from simple substrates, in which the acyl transferase (AT) selects substrates from the bulk cytoplasm. Subsequently, the substrates are transferred by the acyl carrier protein (ACP) robotic arm to the catalytic domains KS, KR, DH, ER forcondensation and processing. Secondary metabolite biosynthetic pathways often proceed separately from the housekeeping functions of a cell. Compartmentalization is achieved by enzyme kinetic phenomena that may rely on dedicated protein architecture and physical proximity. The substrates and cofactors for secondary metabolite biosynthetic pathways are at least partly shared with primary metabolism, and questions remain how resources are distributed among primary and secondary metabolisms. In their Full Paper, F. Stegemann and M. Grininger analyze the process of substrate loading in enzyme kinetic detail, in its substrate selectivity and in its protein‐protein interaction. More information can be found in the Full Paper by F. Stegemann and M. Grininger.