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Docking domain-mediated subunit interactions in natural product megasynth(et)ases

Docking domain-mediated subunit interactions in natural product megasynth(et)ases

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9113145

Docking domain-mediated subunit interactions in natural product megasynth(et)ases

About this item

Full title

Docking domain-mediated subunit interactions in natural product megasynth(et)ases

Publisher

Germany: Oxford University Press

Journal title

Journal of industrial microbiology & biotechnology, 2021-06, Vol.48 (3-4)

Language

English

Formats

Publication information

Publisher

Germany: Oxford University Press

More information

Scope and Contents

Contents

Polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) multienzymes produce numerous high value metabolites. The protein subunits which constitute these megasynth(et)ases must undergo ordered self-assembly to ensure correct organisation of catalytic domains for the biosynthesis of a given natural product. Short amino acid regions at...

Alternative Titles

Full title

Docking domain-mediated subunit interactions in natural product megasynth(et)ases

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9113145

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9113145

Other Identifiers

ISSN

1367-5435,1476-5535

E-ISSN

1476-5535

DOI

10.1093/jimb/kuab018

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