Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate.

scientific article published on 12 December 2008

Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/AEM.01371-08
P932PMC publication ID2643599
P698PubMed publication ID19074611

P50authorKrzysztof PawlikQ73725042
Magdalena KotowskaQ74261551
P2093author name stringKatarzyna Kuczek
Hubert Bartosz-Bechowski
Aleksandra Smulczyk-Krawczyszyn
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Of barn owls and bankers: a lush variety of alpha/beta hydrolasesQ33686427
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Selective removal of aberrant extender units by a type II thioesterase for efficient FR-008/candicidin biosynthesis in Streptomyces sp. strain FR-008.Q36993597
Site-directed mutagenesis studies on the recombinant thioesterase domain of chicken fatty acid synthase expressed in Escherichia coliQ38332420
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Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthaseQ44178730
A catalytic role for histidine 237 in rat mammary gland thioesterase II.Q44321744
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Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated.Q45059780
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Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferaseQ46855747
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Evidence that a novel thioesterase is responsible for polyketide chain release during biosynthesis of the polyether ionophore monensin.Q55042305
Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases.Q55065890
A chain initiation factor common to both modular and aromatic polyketide synthasesQ60301879
The Thioesterase of the Erythromycin-Producing Polyketide Synthase: Influence of Acyl Chain Structure on the Mode of Release of Substrate Analogues from the Acyl Enzyme IntermediatesQ60301902
P433issue4
P407language of work or nameEnglishQ1860
P921main subjectStreptomyces coelicolorQ2355919
P304page(s)887-896
P577publication date2008-12-12
P1433published inApplied and Environmental MicrobiologyQ4781593
P1476titleType II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate
P478volume75

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cites work (P2860)
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