O-acetilhomoserin aminokarboksipropiltransferaza
(Preusmjereno sa stranice O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase)
O-acetilhomoserin aminokarboksipropiltransferaza (EC 2.5.1.49, O-acetil-L-homoserin acetat-lijaza (dodaje metantiol), O-acetil-L-homoserin sulfhidrolaza, O-acetilhomoserin (tiol)-lijaza, O-acetilhomoserinsla sulfhidrolaza, metioninska sintaza) je enzim sa sistematskim imenom O-acetil-L-homoserin:metantiol 3-amino-3-karboksipropiltransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| O-acetilhomoserin aminokarboksipropiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.5.1.49 | ||||||||
| CAS broj | 37290-90-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Ovaj enzim takođe reaguje sa drugim tiolima i H2S, čime se formira homocistein ili tioetri.
Reference uredi
- ↑ Kerr, D. (1971). „O-Acetylhomoserine sulfhydrylase (Neurospora)”. Methods Enzymol. 17B: 446-450.
- ↑ Smith, I.K. and Thompson, J.F. (1969). „Utilization of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies”. Biochim. Biophys. Acta 184: 130-138. PMID 5791104.
- ↑ Yamagata, S. and Takeshima, K. (1976). „O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Further purification and characterization as a pyridoxal enzyme”. J. Biochem. (Tokyo) 80: 777-785. PMID 795806.
- ↑ Yamagata, S. (1976). „O-Acetylserine and O-acetylhomoserine sulfhydrylase of yeast. Subunit structure”. J. Biochem. (Tokyo) 80: 787-797. PMID 795807.
- ↑ Yamagata, S., Takeshima, K. and Naikai, N. (1974). „Evidence for the identity of O-acetylserine sulfhydrylase with O-acetylhomoserine sulfhydrylase in yeast”. J. Biochem. (Tokyo) 75: 1221-1229. PMID 4609980.
- ↑ Yamagata, S. (1989). „Roles of O-acetyl-L-homoserine sulfhydrylases in micro-organisms”. Biochimie 71: 1125-1143. PMID 2517474.
- ↑ Shimizu, H., Yamagata, S., Masui, R., Inoue, Y., Shibata, T., Yokoyama, S., Kuramitsu, S. and Iwama, T. (2001). „Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product”. Biochim. Biophys. Acta 1549: 61-72. PMID 11566369.
Literatura uredi
- 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.