Cystathionine gamma-synthase

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In enzymology, a cystathionine gamma-synthase (EC 2.5.1.48) is an enzyme that catalyzes the chemical reaction

O4-succinyl-L-homoserine + L-cysteine Failed to parse (MathML with SVG or PNG fallback (recommended for modern browsers and accessibility tools): Invalid response ("Math extension cannot connect to Restbase.") from server "https://api.formulasearchengine.com/v1/":): \rightleftharpoons L-cystathionine + succinate

Thus, the two substrates of this enzyme are O4-succinyl-L-homoserine and L-cysteine, whereas its two products are L-cystathionine and succinate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase. Other names in common use include O-succinyl-L-homoserine succinate-lyase (adding cysteine), O-succinylhomoserine (thiol)-lyase, homoserine O-transsuccinylase, O-succinylhomoserine synthase, O-succinylhomoserine synthetase, cystathionine synthase, cystathionine synthetase, homoserine transsuccinylase, 4-O-succinyl-L-homoserine:L-cysteine, and S-(3-amino-3-carboxypropyl)transferase. This enzyme participates in 4 metabolic pathways: methionine metabolism, cysteine metabolism, selenoamino acid metabolism, and sulfur metabolism. It employs one cofactor, pyridoxal phosphate.

References

  • IUBMB entry for 2.5.1.48
  • BRENDA references for 2.5.1.48 (Recommended.)
  • PubMed references for 2.5.1.48
  • PubMed Central references for 2.5.1.48
  • Google Scholar references for 2.5.1.48
  • Flavin M, Slaughter C (1967). "Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine". Biochim. Biophys. Acta. 132: 400–5. PMID 5340123. 
  • Kaplan MM, Flavin M (1966). "Cystathionine gamma-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis". J. Biol. Chem. 241: 4463–71. PMID 5922970. 
  • Wiebers JL, Garner HR (1967). "Homocysteine and cysteine synthetases of Neurospora crassa Purification, properties, and feedback control of activity". J. Biol. Chem. 242: 12–23. PMID 6016326. 
  • Wiebers JL, Garner HR (1967). "Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli". J. Biol. Chem. 242: 5644–9. PMID 12325384. 
  • Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A (1998). "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution". EMBO. J. 17: 6827–38. PMID 9843488. 
  • Ravanel S, Gakiere B, Job D, Douce R (Pt 2). "Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli". Biochem. J. 331: 639–48. PMID 9531508. 

External links

The CAS registry number for this enzyme class is 9030-70-0.

Gene Ontology (GO) codes


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