Peptidna deformilaza
Peptidna deformilaza (EC 3.5.1.88, Peptide deformylase) je enzim sa sistematskim imenom formil-L-metionil peptid amidohidrolaza.[1][2][3][4][5][6][7][8][9][10][11][12] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Peptidna deformilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.1.88 | ||||||||
| CAS broj | 369636-51-1 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- formil-L-metionil peptid + H2O format + metionil peptid
Za dejstvo ovog enzima je neophodno prisustvo Fe(II).
Reference уреди
- ^ Adams, J.M. (1968). „On the release of the formyl group from nascent protein”. J. Mol. Biol. 33: 571—589. PMID 4973445.
- ^ Mazel, D., Pochet, S. and Marliere, P. (1994). „Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation”. EMBO J. 13: 914—923. PMID 8112305.
- ^ Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D. (1997). „Crystal structure of the Escherichia coli peptide deformylase”. Biochemistry. 36: 13904—13909. PMID 9374869.
- ^ Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. (1998). „Structure of peptide deformylase and identification of the substrate binding site”. J. Biol. Chem. 273: 11413—11416. PMID 9565550.
- ^ Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F. (1998). „Iron center, substrate recognition, and mechanism of peptide deformylase”. Nat. Struct. Biol. 5: 1053—1058. PMID 9846875.
- ^ Rajagopalan, P.T.R., Yu, X.C. and Pei, D. (1997). „Peptide deformylase: a new type of mononuclear iron protein”. J. Am. Chem. Soc. 119: 12418—12419.
- ^ Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. (1998). „Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site”. Biochem. Biophys. Res. Commun. 246: 342—346. PMID 9610360.
- ^ Rajagopalan, P.T.R., Grimme, S. and Pei, D. (2000). „Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133”. Biochemistry. 39: 779—790. PMID 10651644.
- ^ Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D. (1999). „Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library”. Biochemistry. 38: 643—650. PMID 9888804.
- ^ Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. (1999). „Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin”. J. Mol. Biol. 289: 1445—1457. PMID 10373378.
- ^ Giglione, C., Pierre, M. and Meinnel, T. (2000). „Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents”. Mol. Microbiol. 36: 1197—1205. PMID 10931273.
- ^ Pei, D. (2001). „Peptide deformylase: a target for novel antibiotics?”. Emerging Therapeutic Targets. 5: 23—40. PMID 15992166.
Literatura уреди
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze уреди
- Peptide+deformylase на US National Library of Medicine Medical Subject Headings (MeSH)
