L-lizin 6-monooksigenaza (NADPH)
L-lizin 6-monooksigenaza (NADPH) (EC 1.14.13.59, lizinska N6-hidroksilaza, L-lizinska 6-monooksigenaza (NADPH) (nespecifična)) je enzim sa sistematskim imenom L-lizin,NADPH:kiseonik oksidoreduktaza (6-hidroksilacija).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-lizin + NADPH + H+ + O2 N6-hidroksi-L-lizin + NADP+ + H2O
Ovaj enzim je flavoprotein (FAD). Enzim iz EN 222 vrste Escherichia coli je visoko specifičan za L-lizin. L-ornitin i L-homolizin nisu supstrati.
Reference
- ^ Plattner, H.J., Pfefferle, P., Romaguera, A., Waschutza, S. and Diekmann, H. (1989). „Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222”. Biol. Met. 2: 1—5. PMID 2518519.
- ^ Macheroux, P., Plattner, H.J., Romaguera, A. and Diekmann, H. (1993). „FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222”. Eur. J. Biochem. 213: 995—1002. PMID 8504838.
- ^ Thariath, A.M., Fatum, K.L., Valvano, M.A. and Viswanatha, T. (1993). „Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase”. Biochim. Biophys. Acta. 1203: 27—35. PMID 8218389.
- ^ de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. (1986). „Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12”. J. Bacteriol. 165: 570—578. PMID 2935523.
- ^ Marrone, L., Siemann, S., Beecroft, M. and Viswanatha, T. (1996). „Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism”. Bioorg. Chem. 24: 401—406.
- ^ Goh, C.J., Szczepan, E.W., Menhart, N. and Viswanatha, T. (1989). „Studies on lysine: N6-hydroxylation by cell-free system of Aerobacter aerogenes 62-1”. Biochim. Biophys. Acta. 990: 240—245. PMID 2493814.
Literatura
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