Lipid IVA 4-amino-4-dezoksi-L-arabinoziltransferaza
Lipid IVA 4-amino-4-dezoksi-L-arabinoziltransferaza (EC 2.4.2.43, undekaprenil fosfat-alfa-L-Ara4N transferaza, 4-amino-4-dezoksi-L-arabinoza lipid A transferaza, protein polimiksinske otpornosti PmrK, arnT (gen)) je enzim sa sistematskim imenom 4-amino-4-dezoksi-alfa-L-arabinopiranozil ditran,oktacis-undekaprenil fosfat:lipid IVA 4-amino-4-dezoksi-L-arabinopiranosiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
Lipid IVA 4-amino-4-dezoksi-L-arabinoziltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.4.2.43 | ||||||||
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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- (1) 4-amino-4-dezoksi-alfa-L-arabinopiranozil ditrans,oktacis-undekaprenil fosfat + alfa-Kdo-(2->4)-alfa-Kdo-(2->6)-lipid A alfa-Kdo-(2->4)-alfa-Kdo-(2->6)-[4-P-L-Ara4N]-lipid A + ditrans,oktacis-undekaprenil fosfat
- (2) 4-amino-4-dezoksi-alfa-L-arabinopiranozil ditrans,oktacis-undekaprenil fosfat + lipid IVA lipid IIA + ditrans,oktacis-undekaprenil fosfat
- (3) 4-amino-4-dezoksi-alfa-L-arabinopiranozil ditrans,oktacis-undekaprenil fosfat + alfa-Kdo-(2->4)-alfa-Kdo-(2->6)-lipid IVA 4'-alfa-L-Ara4N-alfa-Kdo-(2->4)-alfa-Kdo-(2->6)-lipid IVA + ditrans,oktacis-undekaprenil fosfat
Ovaj integralni membranski protein je prisutan na unutrašnjim membranama pojedinih Gram negativnih endobakterija.
Reference
uredi- ↑ Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. (2001). „An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor”. J. Biol. Chem. 276: 43122-43131. PMID 11535604.
- ↑ Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. (2001). „Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm”. J. Biol. Chem. 276: 43132-43144. PMID 11535605.
- ↑ Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. (2001). „Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation”. J. Biol. Chem. 276: 43111-43121. PMID 11535603.
- ↑ Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. (2006). „Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium”. Protein Expr. Purif. 46: 33-39. PMID 16226890.
- ↑ Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. (2010). „Identification of a functionally important loop in Salmonella typhimurium ArnT”. Biochemistry 49: 29-35. PMID 19947657.
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.