Cistationin g-sintaza
(Preusmjereno sa stranice EC 2.5.1.48)
| Cistationin g-sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Cistationin g-sintaza homotetramer, Helicobacter pylori | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.5.1.48 | ||||||||
| CAS broj | 9030-70-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Cistationin g-sintaza (EC 2.5.1.48, O-sukcinil-L-homoserin sukcinat-lijaza (dodaje cistein), O-sukcinilhomoserin (tiol)-lijaza, homoserin O-transsukcinilaza, O-sukcinilhomoserin sintaza, O-sukcinilhomoserin sintetaza, cistationinska sintaza, cistationinska sintetaza, homoserinska transsukcinilaza, 4-O-sukcinil-L-homoserin:L-cistein S-(3-amino-3-karboksipropil)transferaza) je enzim sa sistematskim imenom O4-sukcinil-L-homoserin:L-cistein S-(3-amino-3-karboksipropil)transferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Ovaj enzim je piridoksal-fosfatni protein. On takođe reaguje sa vodonik sulfidom i metantiolom.
Reference[uredi | uredi kod]
- ↑ Flavin, M. and Slaughter, C. (1967). „Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine”. Biochim. Biophys. Acta 132: 400-405. PMID 5340123.
- ↑ Kaplan, M.M. and Flavin, M. (1966). „Cystathionine γ-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis”. J. Biol. Chem. 241: 4463-4471. PMID 5922970.
- ↑ Wiebers, J.L. and Garner, H.R. (1967). „Homocysteine and cysteine synthetases of Neurospora crassa. Purification, properties, and feedback control of activity”. J. Biol. Chem. 242: 12-23. PMID 6016326.
- ↑ Wiebers, J.L. and Garner, H.R. (1967). „Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli”. J. Biol. Chem. 242: 5644-5649. PMID 12325384.
- ↑ Clausen, T., Huber, R., Prade, L., Wahl, M.C. and Messerschmidt, A. (1998). „Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5 Å resolution”. EMBO J. 17: 6827-6838. PMID 9843488.
- ↑ Ravanel, S., Gakiere, B., Job, D. and Douce, R. (1998). „Cystathionine γ-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli”. Biochem. J. 331: 639-648. PMID 9531508.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.