Log in to save to my catalogue

Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3S,4S)...

Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3S,4S)...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_79c28d4ffd014d9f9e4db7231f3c0c7f

Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3S,4S)-3-Amino-4-fluorocyclopentenecarboxylic Acid

About this item

Full title

Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3S,4S)-3-Amino-4-fluorocyclopentenecarboxylic Acid

Publisher

Switzerland: MDPI AG

Journal title

Molecules (Basel, Switzerland), 2023-01, Vol.28 (3), p.1133

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Ornithine aminotransferase (OAT) is overexpressed in hepatocellular carcinoma (HCC), and we previously showed that inactivation of OAT inhibits the growth of HCC. Recently, we found that (3S,4S)-3-amino-4-fluorocyclopentenecarboxylic acid (5) was a potent inactivator of γ-aminobutyric acid aminotransferase (GABA-AT), proceeding by an enamine mechan...

Alternative Titles

Full title

Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3S,4S)-3-Amino-4-fluorocyclopentenecarboxylic Acid

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_79c28d4ffd014d9f9e4db7231f3c0c7f

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_79c28d4ffd014d9f9e4db7231f3c0c7f

Other Identifiers

ISSN

1420-3049

E-ISSN

1420-3049

DOI

10.3390/molecules28031133

How to access this item