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Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition b...

Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition b...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201400069127

Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-γ-linolenic acid

About this item

Full title

Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-γ-linolenic acid

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-09, Vol.108 (38), p.15757-15762

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Human fatty acid synthase (hFAS) is a homodimeric multidomain enzyme that catalyzes a series of reactions leading to the de novo biosynthesis of long-chain fatty acids, mainly palmitate. The carboxy-terminal thioesterase (TE) domain determines the length of the fatty acyl chain and its ultimate release by hydrolysis. Because of the upregulation of...

Alternative Titles

Full title

Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-γ-linolenic acid

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_fao_agris_US201400069127

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201400069127

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1112334108

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