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Natural product reports, ISSN 1460-4752, 2018, Volume 35, Issue 10, pp. 1082 - 1096
Protein–protein interactions of -AT polyketide synthases are dominated by the travels of the ACP domain to the active site entrance of each catalytic domain. 
Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Chemistry, Organic | Life Sciences & Biomedicine | Pharmacology & Pharmacy | Chemistry, Medicinal | Science & Technology | Proteins | Polyketide synthase | Domains | Organic chemistry | Polyketides | Embedded systems | Biosynthesis | Catalysis | Acyltransferase | Protein interaction | Crystallography
Journal Article
2009, 1st ed., Methods in enzymology, ISBN 9780123745880, Volume 458-459., 2 v.
Book
Natural product reports, ISSN 1460-4752, 2016, Volume 33, Issue 2, pp. 231 - 316
This review discusses the biosynthesis of natural products that are generated by -AT polyketide synthases, a family of catalytically versatile enzymes that represents one of the major group... 
Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Chemistry, Organic | Life Sciences & Biomedicine | Pharmacology & Pharmacy | Chemistry, Medicinal | Science & Technology | Biological Products - metabolism | Polyketides - chemistry | Polyketide Synthases - metabolism | Molecular Structure | Humans | Polyketides - metabolism | Index Medicus
Journal Article