TY - JOUR
T1 - Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate
AU - Takano, Eriko
AU - Kotowska, Magdalena
AU - Pawlik, Krzysztof
AU - Smulczyk-Krawczyszyn, Aleksandra
AU - Bartosz-Bechowski, Hubert
AU - Kuczek, Katarzyna
PY - 2009/2
Y1 - 2009/2
N2 - Type II thioesterases (TE IIs) were shown to maintain the efficiency of polyketide synthases (PKSs) by removing acyl residues blocking extension modules. However, the substrate specificity and kinetic parameters of these enzymes differ, which may have significant consequences when they are included in engineered hybrid systems for the production of novel compounds. Here we show that thioesterase ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3(2) is able to hydrolyze acetyl, propionyl, and butyryl residues, which is consistent with its editing function. This enzyme clearly prefers propionate, in contrast to the TE IIs tested previously, and this indicates that it may have a role in control of the starter unit. We also determined activities of ScoT mutants and concluded that this enzyme is an α/β hydrolase with Ser90 and His224 in its active site. Copyright © 2009, American Society for Microbiology. All Rights Reserved.
AB - Type II thioesterases (TE IIs) were shown to maintain the efficiency of polyketide synthases (PKSs) by removing acyl residues blocking extension modules. However, the substrate specificity and kinetic parameters of these enzymes differ, which may have significant consequences when they are included in engineered hybrid systems for the production of novel compounds. Here we show that thioesterase ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3(2) is able to hydrolyze acetyl, propionyl, and butyryl residues, which is consistent with its editing function. This enzyme clearly prefers propionate, in contrast to the TE IIs tested previously, and this indicates that it may have a role in control of the starter unit. We also determined activities of ScoT mutants and concluded that this enzyme is an α/β hydrolase with Ser90 and His224 in its active site. Copyright © 2009, American Society for Microbiology. All Rights Reserved.
KW - 1 nuclease mapping
KW - Disruption mutant complementation
KW - S
KW - Streptomyces fradiae
KW - Thioesterase type II
U2 - 10.1128/AEM.01371-08
DO - 10.1128/AEM.01371-08
M3 - Article
SN - 0099-2240
VL - 75
SP - 887
EP - 896
JO - Applied and environmental microbiology
JF - Applied and environmental microbiology
IS - 4
ER -