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The effect of divalent cations on the thermostability of type II polyketide synthase acyl carrier proteins
Author(s) -
Rivas Marco A.,
Courouble Valentine C.,
Baker Miranda C.,
Cookmeyer David L.,
Fiore Kristen E.,
Frost Alexander J.,
Godbe Kerilyn N.,
Jordan Michael R.,
Krasnow Emily N.,
Mollo Aurelio,
Ridings Stephen T.,
Sawada Keisuke,
Shroff Kavita D.,
Studnitzer Bradley,
Thiele Grace A. R.,
Sisto Ashley C.,
Nawal Saadia,
Huff Adam R.,
Fairman Robert,
Johnson Karl A.,
Beld Joris,
Kokona Bashkim,
Charkoudian Louise K.
Publication year - 2018
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.16402
Subject(s) - thermostability , divalent , chemistry , crystallography , polyketide , denaturation (fissile materials) , protein engineering , protein secondary structure , stereochemistry , biochemistry , enzyme , biosynthesis , organic chemistry , nuclear chemistry
The successful engineering of biosynthetic pathways hinges on understanding the factors that influence acyl carrier protein (ACP) stability and function. The stability and structure of ACPs can be influenced by the presence of divalent cations, but how this relates to primary sequence remains poorly understood. As part of a course‐based undergraduate research experience, we investigated the thermostability of type II polyketide synthase (PKS) ACPs. We observed an approximate 40 °C range in the thermostability among the 14 ACPs studied, as well as an increase in stability (5–26 °C) of the ACPs in the presence of divalent cations. Distribution of charges in the helix II‐loop–helix III region was found to impact the enthalpy of denaturation. Taken together, our results reveal clues as to how the sequence of type II PKS ACPs relates to their structural stability, information that can be used to study how ACP sequence relates to function. © 2018 American Institute of Chemical Engineers AIChE J , 64: 4308–4318, 2018