Mechanism of Inactivation of Ornithine Aminotransferase by (1


Journal

Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056

Informations de publication

Date de publication:
10 07 2019
Historique:
pubmed: 30 6 2019
medline: 23 9 2020
entrez: 29 6 2019
Statut: ppublish

Résumé

The inhibition of ornithine aminotransferase (OAT), a pyridoxal 5'-phosphate-dependent enzyme, has been implicated as a treatment for hepatocellular carcinoma (HCC), the most common form of liver cancer, for which there is no effective treatment. From a previous evaluation of our aminotransferase inhibitors, (1

Identifiants

pubmed: 31251613
doi: 10.1021/jacs.9b03254
pmc: PMC6754100
mid: NIHMS1048343
doi:

Substances chimiques

Carboxylic Acids 0
Cyclopentanes 0
Enzyme Inhibitors 0
Ornithine-Oxo-Acid Transaminase EC 2.6.1.13

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

10711-10721

Subventions

Organisme : NIDA NIH HHS
ID : P30 DA018310
Pays : United States
Organisme : NIDA NIH HHS
ID : R01 DA030604
Pays : United States

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Auteurs

Daniel S Catlin (DS)

Department of Chemistry and Biochemistry , Loyola University Chicago , Chicago , Illinois 60660 , United States.

Dali Liu (D)

Department of Chemistry and Biochemistry , Loyola University Chicago , Chicago , Illinois 60660 , United States.

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Classifications MeSH