2-Halokiselinska dehalogenaza
2-halokiselinska dehalogenaza (EC 3.8.1.2, 2-halokiselinska dehalogenaza (nespecifična), 2-halokiselinska halidohidrolaza (nespecifična), 2-haloalkanoidno kiselinska dehalogenaza, 2-haloalkanoidno kiselinska halidohidrolaza, 2-halokarboksilno kiselinska dehalogenaza II, DL-2-halokiselinska dehalogenaza (nespecifična), L-2-halokiselinska dehalogenaza, L-DEX) je enzim sa sistematskim imenom (S)-2-halokiselina halidohidrolaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
2-halokiselinska dehalogenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.8.1.2 | ||||||||
CAS broj | 37289-39-7 | ||||||||
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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- (S)-2-halokiselina + H2O (R)-2-hidroksikiselina + halid
Ovaj enzim deluje na kiseline sa kratkim lancima, C2 do C4.
Reference
uredi- ↑ Goldman, P., Milne, G.W.A. and Keister, D.B. (1968). „Carbon-halogen bond cleavage. 3. Studies on bacterial halidohyrolases”. J. Biol. Chem. 243: 428-434. PMID 5635785.
- ↑ Motosugi, M., Esaki, N. and Soda, K. (1982). „Preparation and properties of 2-halo acid dehalogenase from Pseudomonas putida”. Agric. Biol. Chem. 46: 837-838.
- ↑ Klages, M., Krauss, S. and Lingens, F. (1983). „2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3”. Hoppe-Seyler's Z. Physiol. Chem. 364: 529-535. PMID 6873881.
- ↑ Diez, A., Prieto, M.I., Alvarez, M.J., Bautista, J.M., Garrido, J. and Puyet, A. (1996). „Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation”. Biochem. Biophys. Res. Commun. 220: 828-833. PMID 8607850.
- ↑ Mörsberger, F.-M., Müller, R., Otto, M.K., Lingens, F. and Kulbe, K.D. (1991). „Purification and characterization of 2-halocarboxylic acid dehalogenase II from Pseudomonas spec. CBS 3”. Biol. Chem. Hoppe-Seyler 372: 915-922. PMID 1772590.
- ↑ Köhler, R., Brokamp, A., Schwarze, R., Reiting, R.H. and Schmidt, F.R.J. (1998). „Characteristics and DNA-sequence of a cryptic haloalkanoic acid dehalogenase from Agrobacterium tumefaciens RS5”. Curr. Microbiol. 36: 96-101. PMID 9425247.
- ↑ Motosugi, K., Esahi, N. and Soda, K. (1982). „Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase”. Arch. Microbiol. 131: 179-183. PMID 7103659.
- ↑ Kurihara, T., Esaki, N. and Soda, K. (2000). „Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms”. J. Mol. Catal., B Enzym. 10: 57-65.
- ↑ Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi, M., Tsunasawa, S. and Esaki, N. (1996). „Bacterial 2-haloacid dehalogenases: Structures and catalytic properties”. Pure Appl. Chem. 68: 2097-2103.
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.