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Thiolutin Is a Zinc Chelator That Inhibits the Rpn11 and Other JAMM Metalloproteases

Thiolutin Is a Zinc Chelator That Inhibits the Rpn11 and Other JAMM Metalloproteases

Linda Lauinger, Jing Li, Anton Shostak, Ibrahim Avi Cemel, Nati Ha, Yaru Zhang, Philipp E Merkl, Simon Obermeyer, Nicolas Stankovic-Valentin, Tobias Schafmeier, Walter J Wever, Albert A Bowers, Kyle P Carter, etc.

Nat Chem Biol. 2017 Jul;13(7):709-714.

PMID: 28459440

Abstract:

Thiolutin is a disulfide-containing antibiotic and anti-angiogenic compound produced by Streptomyces. Its biological targets are not known. We show that reduced thiolutin is a zinc chelator that inhibits the JAB1/MPN/Mov34 (JAMM) domain-containing metalloprotease Rpn11, a deubiquitinating enzyme of the 19S proteasome. Thiolutin also inhibits the JAMM metalloproteases Csn5, the deneddylase of the COP9 signalosome; AMSH, which regulates ubiquitin-dependent sorting of cell-surface receptors; and BRCC36, a K63-specific deubiquitinase of the BRCC36-containing isopeptidase complex and the BRCA1-BRCA2-containing complex. We provide evidence that other dithiolopyrrolones also function as inhibitors of JAMM metalloproteases.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP87116	Thiolutin		87-11-6	Price

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