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Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile...

Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b11a9305566844e8ac7e9252b972e34e

Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile enzymes

About this item

Full title

Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile enzymes

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2025-03, Vol.16 (1), p.2949-12, Article 2949

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Proteases are defined by their nucleophile but require additional residues to regulate their active sites, most often arranged as catalytic triads that control the generation and resolution of acyl-enzyme intermediates. Threonine N-terminal nucleophiles represent a diverse family of proteases and transferases that possess two active site nucleophil...

Alternative Titles

Full title

Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile enzymes

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_b11a9305566844e8ac7e9252b972e34e

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b11a9305566844e8ac7e9252b972e34e

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-025-58077-x

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