| EC |
2.5.1.48 |
| Accepted name: |
cystathionine γ-synthase |
| Reaction: |
O4-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate |
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For diagram of reaction, click here |
| Other name(s): |
O-succinyl-L-homoserine succinate-lyase (adding cysteine); O-succinylhomoserine (thiol)-lyase; homoserine O-transsuccinylase (ambiguous); O-succinylhomoserine synthase; O-succinylhomoserine synthetase; cystathionine synthase; cystathionine synthetase; homoserine transsuccinylase (ambiguous); 4-O-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase |
| Systematic name: |
O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase |
| Comments: |
A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse β,γ-elimination to form 2-oxobutanoate, succinate and ammonia. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-70-0 |
| References: |
| 1. |
Flavin, M. and Slaughter, C. Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine. Biochim. Biophys. Acta 132 (1967) 400–405. [DOI] [PMID: 5340123] |
| 2. |
Kaplan, M.M. and Flavin, M. Cystathionine γ-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis. J. Biol. Chem. 241 (1966) 4463–4471. [PMID: 5922970] |
| 3. |
Wiebers, J.L. and Garner, H.R. Homocysteine and cysteine synthetases of Neurospora crassa. Purification, properties, and feedback control of activity. J. Biol. Chem. 242 (1967) 12–23. [PMID: 6016326] |
| 4. |
Wiebers, J.L. and Garner, H.R. Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli. J. Biol. Chem. 242 (1967) 5644–5649. [PMID: 12325384] |
| 5. |
Clausen, T., Huber, R., Prade, L., Wahl, M.C. and Messerschmidt, A. Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5 Å resolution. EMBO J. 17 (1998) 6827–6838. [DOI] [PMID: 9843488] |
| 6. |
Ravanel, S., Gakiere, B., Job, D. and Douce, R. Cystathionine γ-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli. Biochem. J. 331 (1998) 639–648. [PMID: 9531508] |
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| [EC 2.5.1.48 created 1972 as EC 4.2.99.9, transferred 2002 to EC 2.5.1.48] |
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