Cited by 436Amino Acid Enzymes and MetabolismPolyamine Metabolism and ApplicationsCancer-related gene regulation

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Arginine Metabolism Revisited

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Morris, Sidney M·2016·The Journal of Nutrition

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Abstract

Mammalian arginine metabolism is complex due to the expression of multiple enzymes that utilize arginine as substrate and to interactions or competition between specific enzymes involved in arginine metabolism. Moreover, cells may contain multiple intracellular arginine pools that are not equally accessible to all arginine metabolic enzymes, thus presenting additional challenges to more fully understanding arginine metabolism. At the whole-body level, arginine metabolism ultimately results in the production of a biochemically diverse range of products, including nitric oxide, urea, creatine, polyamines, proline, glutamate, agmatine, and homoarginine. Included in this group of compounds are the methylated arginines (e.g., asymmetric dimethylarginine), which are released upon degradation of proteins containing methylated arginine residues. Changes in arginine concentration also can regulate cellular metabolism and function via a variety of arginine sensors. Although much is known about arginine metabolism, elucidation of the physiologic or pathophysiologic roles for all of the pathways and their metabolites remains an active area of investigation, as exemplified by current findings highlighted in this review.

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Additional file 2 of Changes of microbial and metabolome of the equine hindgut during oligofructose-induced laminitis
Tuniyazi, M., He, J., Guo, J., Li, S., Zhang, N., Hu, X., & Fu, Y. (2021) · Figshare · doi:10.6084/m9.figshare.13532320
Additional file 3 of Changes of microbial and metabolome of the equine hindgut during oligofructose-induced laminitis
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Additional file 4 of Changes of microbial and metabolome of the equine hindgut during oligofructose-induced laminitis
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Authors: Morris, S. M.
Affiliations: University of Pittsburgh (US)
Corresponding author: Morris, Sidney M
ORCID: Morris, Sidney M
Venue: The Journal of Nutrition
Publisher: Elsevier BV
Published: 2016-12
Volume: 146
Issue: 12
Pages: 2579S-2586S
ISSN: 0022-3166 (ISSN-L)
DOI: 10.3945/jn.115.226621
OpenAlex: W2555868191
Cited by: 435
References: 122
Citations by year: 2026: 61 · 2025: 69 · 2024: 48 · 2023: 64 · 2022: 52 · 2021: 58 · 2020: 35 · 2019: 24 · 2018: 16 · 2017: 7
FWCI: 1.97
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2248 d)
Locations: Journal of Nutrition (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
Keywords: arginine metabolism, nitric oxide, urea, creatine, polyamines, proline, glutamate, agmatine, homoarginine, asymmetric dimethylarginine, enzyme competition, protein degradation
MeSH terms: Animals, Arginine, Mammals

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