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Article

The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study.

Proceedings of the National Academy of Sciences of the United States of America - 28 Sept 1999

Groll M, Heinemeyer W, Jäger S, Ullrich T, Bochtler M, Wolf D H, Huber R

Abstract excerpt

We present a biochemical and crystallographic characterization of active site mutants of the yeast 20S proteasome with the aim to characterize substrate cleavage specificity, subunit intermediate processing, and maturation. beta1(Pre3), beta2(Pup1), and beta5(Pre2) are responsible for the postacidic, tryptic, and chymotryptic activity, respectively. The maturation of active subunits is independent of the presence...

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Identifiers

PMID: 10500111
DOI: 10.1073/pnas.96.20.10976
PMCID: PMC34229

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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