Kvorum-sensing N-acil-homoserinska laktonaza
Kvorum-sensing N-acil-homoserinska laktonaza (EC 3.1.1.81, acil homoserin degradirajući enzim, acil-homoserin laktonska acilaza, AHL laktonaza, AHL-degradirajući enzim, AHL-inaktivirajući enzim, AHLaza, AhlD, AhlK, AiiA, AiiA laktonaza, AiiA-sličan protein, AiiB, AiiC, AttM, delaktonaza, laktonazi sličan enzim, N-acil homoserin laktonaza, N-acil homoserin laktonska hidrolaza, N-acil-homoserin laktonska laktonaza, N-acil-L-homoserin laktonska hidrolaza, kvorum-sensing laktonaza, kvorum-sensing N-acil homoserin laktonska hidrolaza) je enzim sa sistematskim imenom N-acil-L-homoserin-lakton laktonohidrolaza.[1][2][3][4][5][6][7][8][9][10][11] Ovaj enzim katalizuje sledeću hemijsku reakciju
Kvorum-sensing N-acil-homoserinska laktonaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 3.1.1.81 | ||||||||
CAS broj | 389867-43-0 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
- N-acil-L-homoserin lakton + H2O N-acil-L-homoserin
Acil-homoserinske laktone (AHL) formiraju gram negativne bakterije i obično ih koriste kao signalni molekul za međusobnu komunikaciju u procesu kvorum-sensinga. AHL se vezuje za transkripcione faktore i na taj način utiče na ekspresiju gena. Ovim vidom komunikacije bakterije regulišu brojne biološke funkcije, uključujući i sekreciju faktora virulencije.
Reference uredi
- ↑ Thomas, P.W., Stone, E.M., Costello, A.L., Tierney, D.L. and Fast, W. (2005). „The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein”. Biochemistry 44: 7559-7569. PMID 15895999.
- ↑ Dong, Y.H., Gusti, A.R., Zhang, Q., Xu, J.L. and Zhang, L.H. (2002). „Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species”. Appl. Environ. Microbiol. 68: 1754-1759. PMID 11916693.
- ↑ Wang, L.H., Weng, L.X., Dong, Y.H. and Zhang, L.H. (2004). „Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase)”. J. Biol. Chem. 279: 13645-13651. PMID 14734559.
- ↑ Dong, Y.H., Xu, J.L., Li, X.Z. and Zhang, L.H. (2000). „AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora”. Proc. Natl. Acad. Sci. USA 97: 3526-3531. PMID 10716724.
- ↑ Dong, Y.H., Wang, L.H., Xu, J.L., Zhang, H.B., Zhang, X.F. and Zhang, L.H. (2001). „Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase”. Nature 411: 813-817. PMID 11459062.
- ↑ Lee, S.J., Park, S.Y., Lee, J.J., Yum, D.Y., Koo, B.T. and Lee, J.K. (2002). „Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis”. Appl. Environ. Microbiol. 68: 3919-3924. PMID 12147491.
- ↑ Park, S.Y., Lee, S.J., Oh, T.K., Oh, J.W., Koo, B.T., Yum, D.Y. and Lee, J.K. (2003). „AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria”. Microbiology 149: 1541-1550. PMID 12777494.
- ↑ Ulrich, R.L. (2004). „Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis”. Appl. Environ. Microbiol. 70: 6173-6180. PMID 15466564.
- ↑ Kim, M.H., Choi, W.C., Kang, H.O., Lee, J.S., Kang, B.S., Kim, K.J., Derewenda, Z.S., Oh, T.K., Lee, C.H. and Lee, J.K. (2005). „The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase”. Proc. Natl. Acad. Sci. USA 102: 17606-17611. PMID 16314577.
- ↑ Liu, D., Lepore, B.W., Petsko, G.A., Thomas, P.W., Stone, E.M., Fast, W. and Ringe, D. (2005). „Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis”. Proc. Natl. Acad. Sci. USA 102: 11882-11887. PMID 16087890.
- ↑ Yang, F., Wang, L.H., Wang, J., Dong, Y.H., Hu, J.Y. and Zhang, L.H. (2005). „Quorum quenching enzyme activity is widely conserved in the sera of mammalian species”. FEBS Lett. 579: 3713-3717. PMID 15963993.
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.