Galaktofuranozilgalaktofuranozilramnozil-N-acetilglukozaminil-difosfo-dekaprenol beta-1,5/1,6-galaktofuranoziltransferaza
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| Galaktofuranozilgalaktofuranozilramnozil-N-acetilglukozaminil-difosfo-dekaprenol beta-1,5/1,6-galaktofuranoziltransferaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 2.4.1.288 | ||||||||
| 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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Galaktofuranozilgalaktofuranozilramnozil-N-acetilglukozaminil-difosfo-dekaprenol beta-1,5/1,6-galaktofuranoziltransferaza (EC 2.4.1.288, GlfT2) je enzim sa sistematskim imenom UDP-alfa-D-galaktofuranoza:beta-D-galaktofuranozil-(1->5)-beta-D-galaktofuranozil-(1->4)-alfa-L-ramnopiranozil-(1->3)-N-acetil-alfa-D-glukozaminil-difosfo-trans,oktacis-dekaprenol 4-beta/5-beta-D-galaktofuranoziltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 28 UDP-alfa-D-galaktofuranoza + beta-D-galaktofuranozil-(1->5)-beta-D-galaktofuranozil-(1->4)-alfa-L-ramnopiranozil-(1->3)-N-acetil-alfa-D-glukozaminil-difosfo-trans,oktacis-dekaprenol 28 UDP + [beta-D-galaktofuranozil-(1->5)-beta-D-galaktofuranozil-(1->6)]14-beta-D-galaktofuranozil-(1->5)-beta-D-galaktofuranozil-(1->4)-alfa-L-ramnopiranozil-(1->3)-N-acetil-alfa-D-glukozaminil-difosfo-trans,oktacis-dekaprenol
Ovaj enzim je izolovan iz Mycobakterija tuberculosis. On dodaje aproksimativno dvadest osam galaktofuranozilnih ostataka sa naizmeničnim 1->5 i 1->6 vezama čime se formira galaktanski domen.
Reference[uredi | uredi kod]
- ↑ Rose, N.L., Zheng, R.B., Pearcey, J., Zhou, R., Completo, G.C. and Lowary, T.L. (2008). „Development of a coupled spectrophotometric assay for GlfT2, a bifunctional mycobacterial galactofuranosyltransferase”. Carbohydr. Res. 343: 2130-2139. PMID 18423586.
- ↑ May, J.F., Splain, R.A., Brotschi, C. and Kiessling, L.L. (2009). „A tethering mechanism for length control in a processive carbohydrate polymerization”. Proc. Natl. Acad. Sci. USA 106: 11851-11856. PMID 19571009.
- ↑ Wheatley, R.W., Zheng, R.B., Richards, M.R., Lowary, T.L. and Ng, K.K. (2012). „Tetrameric structure of GlfT2 reveals a scaffold for the assembly of mycobacterial arabinogalactan”. J. Biol. Chem.: -. PMID 22707726.
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.