2,3-Dihidroksibenzoat-serinska ligaza
| 2,3-Dihidroksibenzoat-serinska ligaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 6.3.2.14 | ||||||||
| CAS broj | 37318-63-1 | ||||||||
| 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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2,3-Dihidroksibenzoat-serinska ligaza (EC 6.3.2.14, N-(2,3-dihidroksibenzoil)-serin sintetaza, 2,3-dihidroksibenzoilserin sintetaza, 2,3-dihidroksibenzoat—serin ligaza) je enzim sa sistematskim imenom 2,3-dihidroksibenzoat:L-serin ligaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Ovaj enzimski kompleks katalizuje konverziju molekula koji se formiraju siderofori enterobaktina.
- ↑ Brot, N. and Goodwin, J. (1968). „Regulation of 2,3-dihydroxybenzoylserine synthetase by iron”. J. Biol. Chem. 243: 510-513. PMID 4966114.
- ↑ Rusnak, F., Faraci, W.S. and Walsh, C.T. (1989). „Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product”. Biochemistry 28: 6827-6835. PMID 2531000.
- ↑ Rusnak, F., Liu, J., Quinn, N., Berchtold, G.A. and Walsh, C.T. (1990). „Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase”. Biochemistry 29: 1425-1435. PMID 2139796.
- ↑ Rusnak, F., Sakaitani, M., Drueckhammer, D., Reichert, J. and Walsh, C.T. (1991). „Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine”. Biochemistry 30: 2916-2927. PMID 1826089.
- ↑ Gehring, A.M., Mori, I. and Walsh, C.T. (1998). „Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF”. Biochemistry 37: 2648-2659. PMID 9485415.
- ↑ Shaw-Reid, C.A., Kelleher, N.L., Losey, H.C., Gehring, A.M., Berg, C. and Walsh, C.T. (1999). „Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization”. Chem. Biol. 6: 385-400. PMID 10375542.
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- 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.