Role of carnosine in muscle contraction (WP4486)

Homo sapiens

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Carnosine is known to be an antioxidant, a metal chelator, a Ca(2+) and enzyme regulator. It also functions as an inhibitor of protein glycosylation and protein-protein cross-linking. Carnosine has also been linked to overcoming muscle fatigue, and can only be transported into a working muscle cell. This pathway shows the main metabolites of carnosine and their relationship with each other.

Authors

Denise Slenter , Egon Willighagen , Kristina Hanspers , Alex Pico , Eric Weitz , and Finterly Hu

Activity

last edited

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Cited In

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Organisms

Homo sapiens

Communities

Annotations

Pathway Ontology

histidine degradation pathway

Cell Type Ontology

muscle cell

Participants

Label Type Compact URI Comment
Carnosine Metabolite wikidata:Q413822
beta-alanine Metabolite wikidata:Q310919 'Indispensable component of coenzyme A'
'Product of pyrimidine base degradation'
'Factor which stimulates collagen synthesis in tissues'
Carcinine Metabolite wikidata:Q27892933
histamine Metabolite wikidata:Q61233
Histidine Metabolite wikidata:Q485277
Carnosine Metabolite wikidata:Q413822
Ophidine Metabolite pubchem.compound:90658938 aka beta-alanyl-3-N-methylhistidine
Anserine Metabolite wikidata:Q415335
Acetylcarnosine Metabolite wikidata:Q4673297 Found in Myocardial tissue
Homocarnosine Metabolite wikidata:Q27158831
Homoanserine Metabolite pubchem.compound:20849429
gamma-aminobutyric acid Metabolite wikidata:Q210021
carnosinase Protein eccode:3.4.13.3 Specific enzyme for carnosine breakdown (not specified in literature for which reaction).
'This enzyme is present in considerable quantity in many tissues (with the exception of skeletal musculature) and is especially abundant in the kidney, liver and blood plasma '
carnosine synthetase Protein eccode:6.3.2.11

References

  1. Detection, characterisation, and quantification of carnosine and other histidyl derivatives in cardiac and skeletal muscle. O’Dowd JJ, Robins DJ, Miller DJ. Biochimica et Biophysica Acta (BBA) - General Subjects [Internet]. 1988 Nov;967(2):241–9. Available from: http://dx.doi.org/10.1016/0304-4165(88)90015-3 DOI Scholia
  2. The histidine-containing dipeptides, carnosine and anserine: distribution, properties and biological significance. Boldyrev AA, Severin SE. Adv Enzyme Regul. 1990;30:175–94. PubMed Europe PMC Scholia
  3. Realization of spontaneous healing function by carnosine. Nagai K, Suda T. Methods Find Exp Clin Pharmacol. 1988 Aug;10(8):497–507. PubMed Europe PMC Scholia
  4. Dietary regulation of intestinal transport of the dipeptide carnosine. Ferraris RP, Diamond J, Kwan WW. Am J Physiol. 1988 Aug;255(2 Pt 1):G143-50. PubMed Europe PMC Scholia
  5. Carnosinase and homocarnosinosis. Lenney JF. J Oslo City Hosp. 1985;35(2–3):27–40. PubMed Europe PMC Scholia
  6. Intensity of biosynthesis of anserine and carnosine by intact and denervated muscles in chickens. Dobrynina OV, Gorbunova AV. Biokhimiia. 1968;33(3):570–5. PubMed Europe PMC Scholia
  7. Hydrolysis of carnosine and related compounds by mammalian carnosinases. Pegova A, Abe H, Boldyrev A. Comp Biochem Physiol B Biochem Mol Biol. 2000 Dec;127(4):443–6. PubMed Europe PMC Scholia
  8. Physiological role of carnosine in contracting muscle. Begum G, Cunliffe A, Leveritt M. Int J Sport Nutr Exerc Metab. 2005 Oct;15(5):493–514. PubMed Europe PMC Scholia