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Article

Insights on the participation of Glu256 and Asp204 in the oligomeric structure and cooperative effects of human arginase type I.

Journal of structural biology - 1 Aug 2020

Lobos Marcela, Figueroa Maximiliano, Martínez-Oyanedel José, López Vasthi, García-Robles María de Los Ángeles, Tarifeño-Saldivia Estefanía, Carvajal Nelson, Uribe Elena

Abstract excerpt

Arginase (EC 3.5.3.1) catalyzes the hydrolysis of L-arginine to L-ornithine and urea, and requires a bivalent cation, especially Mn2+ for its catalytic activity. It is a component of the urea cycle and regulates the intracellular levels of l-arginine, which makes the arginase a target for treatment of vascular diseases and asthma. Mammalian arginases contain an unusual S-shaped motif located at the intermonomeric...

Topics

Arginase
Arginine
Aspartic Acid
Glutamic Acid
Humans
Kinetics
Macromolecular Substances
Models, Molecular
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Multimerization

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Identifiers

PMID: 32450233
DOI: 10.1016/j.jsb.2020.107533

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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