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Cysteine metabolism
Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.
Human cysteine metabolism
In human cysteine metabolism, L-cysteine is consumed in several ways as shown below. L-Cysteine is also consumed in pantothenate/coenzyme A biosynthesis.
| Enzyme | → | Products | Cofactor/Additional Reactant | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| cysteine dioxygenase | → | cysteine sulfinic acid | iron | |||||||||||
| serine racemase | → | D-cysteine | pyridoxal phosphate | |||||||||||
| cysteine lyase | → | L-cysteate/hydrogen sulfide | pyridoxal phosphate/sulfite | |||||||||||
| vauthors = Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, van-den-Berg S, Deng LW, Moore PK, Karlberg T, Sivaraman J | display-authors = 6 | title = Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S | language = English | journal = The Journal of Biological Chemistry | volume = 284 | issue = 5 | pages = 3076–3085 | date = January 2009 | pmid = 19019829 | doi = 10.1074/jbc.M805459200 | doi-access = free }} | → | pyruvate/NH3/H2S | pyridoxal phosphate |
| cysteine—tRNA ligase | → | L-cysteinyl-tRNACys | ||||||||||||
| cystine reductase | → | L-cystine/NADH and H+ | NAD+ | |||||||||||
| vauthors = Hipólito A, Nunes SC, Vicente JB, Serpa J | title = Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer | journal = Molecules | volume = 25 | issue = 17 | page = 3984 | date = September 2020 | pmid = 32882966 | pmc = 7504796 | doi = 10.3390/molecules25173984 | doi-access = free }} | → | [3-mercapto-pyruvate](3-mercapto-pyruvate)/L-glutamate | pyridoxal phosphate/alpha-ketoglutaric acid | |
| glutamate–cysteine ligase | → | γ-glutamyl cysteine/ADP and Pi | ATP |
L-Cysteine is the product of several processes as well. In addition to the reactions below, L-cysteine is also a product of glycine, serine, and threonine metabolism.
| Reactants | → | Enzyme | Cofactors | Notes |
|---|---|---|---|---|
| *O*-acetyl-L-serine/hydrogen sulfide | → | cysteine synthase | pyridoxal phosphate | not present in humans |
| L-cystine/2 glutathione | → | glutathione-cystine transhydrogenase | ||
| cystathionine | → | cystathionine γ-lyase | pyridoxal phosphate | |
| [3-mercapto-pyruvate](3-mercapto-pyruvate) | → | cysteine transaminase | pyridoxal phosphate |
References
References
- (May 2009). "Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels". Amino Acids.
- (March 2023). "Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids". Chirality.
- (February 1969). "Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo". Biochimica et Biophysica Acta (BBA) - Enzymology.
- (January 2009). "Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S". The Journal of Biological Chemistry.
- (December 1964). "The separation and partial purification of aminoacyl-RNA synthetases from Escherichia coli". Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects.
- (September 1978). "Cystine reductase in the dimorphic fungus Histoplasma capsulatum". Journal of Bacteriology.
- (September 2020). "Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer". Molecules.
- (October 2005). "Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels". The Journal of Biological Chemistry.
- (May 1969). "Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium". The Journal of Biological Chemistry.
- (April 1968). "A thiol-disulfide transhydrogenase from yeast". The Journal of Biological Chemistry.
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