4-Hidroksibenzoat 3-monooksigenaza
4-hidroksibenzoat 3-monooksigenaza (EC 1.14.13.2, p-hidroksibenzoatna hidrolijaza, p-hidroksibenzoatna hidroksilaza, 4-hidroksibenzoatna 3-hidroksilaza, 4-hidroksibenzoatna monooksigenaza, 4-hidroksibenzoinska hidroksilaza, p-hidroksibenzoat-3-hidroksilaza, p-hidroksibenzojeva kiselina hidrolaza, p-hidroksibenzojeva hidroksilaza) je enzim sa sistematskim imenom 4-hidroksibenzoat,NADPH:kiseonik oksidoreduktaza (3-hidroksilacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
4-hidroksibenzoat 3-monooksigenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.14.13.2 | ||||||||
CAS broj | 9059-23-8 | ||||||||
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 | ||||||||
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- 4-hidroksibenzoat + NADPH + H+ + O2 protokatehuat + NADP+ + H2O
Ovaj enzim je flavoprotein (FAD). Većina enzima iz Pseudomonas su visoko specifični za NADPH (cf. EC 1.14.13.33, 4-hidroksibenzoat 3-monooksigenaza [NAD(P)H]).
Reference
uredi- ^ Hosokawa, K. & Stanier, R.Y. (1966). „Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida”. J. Biol. Chem. 241: 2453—2460. PMID 4380381.
- ^ Howell, L.G., Spector, T. and Massey, V. (1972). „Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens”. J. Biol. Chem. 247: 4340—4350. PMID 4402514.
- ^ Spector, T. & Massey, V. (1972). „Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens”. J. Biol. Chem. 247: 4679—4687. PMID 4402938.
- ^ Spector, T. & Massey, V. (1972). „p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate”. J. Biol. Chem. 247: 5632—5636. PMID 4403446.
- ^ Spector, T. & Massey, V. (1972). „p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen”. J. Biol. Chem. 247: 7123—7127. PMID 4404745.
- ^ Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J. and Muller, R. (1996). „4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity”. Eur. J. Biochem. 239: 469—478. PMID 8706756.
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.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
uredi- 4-hydroxybenzoate+3-monooxygenase na US National Library of Medicine Medical Subject Headings (MeSH)