The DOI matches its Crossref record; 24 of the 26 references it cites were found in a registry or an index.
Structure of a unique binuclear manganese cluster in arginase
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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“Each domain adopted the α/β-fold first observed in the crystal structure of arginase25 and subsequently observed in the HDAC family26.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [25]
In the citing paper
“As previously mentioned, HDACs adopt the same α/β-fold first observed in the crystal structure of arginase, a binuclear manganese metalloenzyme that catalyses the hydrolysis of arginine to form ornithine plus urea1525.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [25]
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Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
New developments in RiPP discovery, enzymology and engineering
Montalbán‐López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2020) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 775
Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases
Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710
Arginase: an emerging key player in the mammalian immune system
Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 725
Physiological implications of arginine metabolism in plants
Winter, G., Todd, C. D., Trovato, M., Forlani, G., & Funck, D. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00534 · Cited by 652
Metadata
- Authors
- Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W.
- Affiliations
- University of Pennsylvania (US)
- Temple University (US)
- Venue
- Nature
- Published
- 1996-10
- Volume
- 383
- Issue
- 6600
- Pages
- 554-557
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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