Cited by 450Enzyme Structure and FunctionAmino Acid Enzymes and MetabolismMetal-Catalyzed Oxygenation Mechanisms

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Structure of a unique binuclear manganese cluster in arginase

Kanyo, Zoltan F., Scolnick, Laura R., Ash, David E., Christianson, David W.·1996·Nature

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Abstract

Each individual excretes roughly 10 kg of urea per year, as a result of the hydrolysis of arginine in the final cytosolic step of the urea cycle. This reaction allows the disposal of nitrogenous waste from protein catabolism, and is catalysed by the liver arginase enzyme. In other tissues that lack a complete urea cycle, arginase regulates cellular arginine and ornithine concentrations for biosynthetic reactions, including nitric oxide synthesis: in the macrophage, arginase activity is reciprocally coordinated with that of NO synthase to modulate NO-dependent cytotoxicity. The bioinorganic chemistry of arginase is particularly rich because this enzyme is one of very few that specifically requires a spin-coupled Mn2+-Mn2+ cluster for catalytic activity in vitro and in vivo. The 2.1 angstrom-resolution crystal structure of trimeric rat liver arginase reveals that this unique metal cluster resides at the bottom of an active-site cleft that is 15 angstroms deep. Analysis of the structure indicates that arginine hydrolysis is achieved by a metal-activated solvent molecule which symmetrically bridges the two Mn2+ ions.

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Authors: Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W.
Affiliations: University of Pennsylvania (US)
Temple University (US)
ORCID: Christianson, David W.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1996-10
Volume: 383
Issue: 6600
Pages: 554-557
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/383554a0
OpenAlex: W2066916400
Cited by: 441
References: 26
Citations by year: 2026: 18 · 2025: 6 · 2024: 18 · 2023: 12 · 2022: 9 · 2021: 8 · 2020: 17 · 2019: 15 · 2018: 15 · 2017: 14 · 2016: 8 · 2015: 13 · 2014: 11 · 2013: 18 · 2012: 15
FWCI: 15.87
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (R01GM067788)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: arginase, urea cycle, arginine hydrolysis, crystal structure, metalloenzyme active site, nitric oxide production, enzyme catalysis
MeSH terms: Animals, Arginase, Arginine, Binding Sites, Liver, Manganese, Metalloproteins, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Crystallography, X-Ray, Rats

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Structure of a unique binuclear manganese cluster in arginase

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