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Published in 2022 at "Chembiochem"
DOI: 10.1002/cbic.202200200
Abstract: The ketosynthase (KS) domain is a core domain found in modular polyketide synthases (PKSs). To maintain the polyketide biosynthetic fidelity, the KS domain must only accept an acyl group from the acyl carrier protein (ACP)…
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Keywords:
protein protein;
domain;
transacylation;
transacylation reaction ... See more keywords
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Published in 2018 at "Journal of structural biology"
DOI: 10.1016/j.jsb.2018.04.001
Abstract: Ketoreductase (KR) domains of modular polyketide synthases (PKSs) control the stereochemistry of C2 methyl and C3 hydroxyl substituents of polyketide intermediates. To understand the molecular basis of stereocontrol exerted by KRs, the crystal structure of…
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Keywords:
polyketide;
structures ketoreductase;
bound structures;
substrate bound ... See more keywords
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Published in 2020 at "Synthetic and Systems Biotechnology"
DOI: 10.1016/j.synbio.2020.04.001
Abstract: Modular polyketide synthases (PKSs) are a multidomain megasynthase class of biosynthetic enzymes that have great promise for the development of new compounds, from new pharmaceuticals to high value commodity and specialty chemicals. Their colinear biosynthetic…
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Keywords:
protein;
synthetic biology;
modular polyketide;
biology ... See more keywords
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Published in 2022 at "Biochemistry"
DOI: 10.1021/acs.biochem.2c00645
Abstract: Acyltransferase (AT) recognizes its cognate acyl carrier protein (ACP) for functional transfer of an acyl unit in polyketide biosynthesis. However, structural characterization of AT-ACP complexes is limited because of the weak and transient interactions between…
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Keywords:
vink;
vink vinp1acpl;
transient interactions;
acp ... See more keywords