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Article

The activation loop and substrate-binding cleft of glutaminase C are allosterically coupled.

The Journal of biological chemistry - 31 Jan 2020

Li Yunxing, Ramachandran Sekar, Nguyen Thuy-Tien T, Stalnecker Clint A, Cerione Richard A, Erickson Jon W

Abstract excerpt

The glutaminase C (GAC) isoform of mitochondrial glutaminase is overexpressed in many cancer cells and therefore represents a potential therapeutic target. Understanding the regulation of GAC activity has been guided by the development of spectroscopic approaches that measure glutaminase activity in real time. Previously, we engineered a GAC protein (GAC(F327W)) in which a tryptophan residue is substituted for...

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Identifiers

PMID: 31871054
DOI: 10.1074/jbc.RA119.010314
PMCID: PMC6996896

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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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