Lysine oxygenase

The following is review on the molecular and physical properties of this class of monooxygenases, which are also known as hydroxylases. A typical monooxygenase reaction is the hydroxylation of an alkane to an alcohol which involves a reduced cosubstrate that reduces a second atom within the O2 molecule to form water. Flavin-containing monooxygenases include lysine oxygenase and 4-hydroxybenzoate hydroxylase. Reduced pteri-dines are involved in the phenylalanine hydroxylase and tryptophan hydroxylase reactions. See also Cytochrome P-450... 

Degradation of L-arginine by Streptomyces griseus is initiated by a hydroxylase that causes decarboxylation and conversion of the amino acid into an amide (Eq. 24-26), a reaction analogous to that catalyzed by the flavin-dependent lysine oxygenase (Eq. 18-41). The... 

Lysine oxygenase Pseudomonas Lysine S-Aminovaleric acid COj, NH, Itada et al. (1961)... 

Lairtic acid oxygenase Inositol oxygenase Lysine oxygenase... 

Enzymatic hydroxylation of biological molecules is often catalyzed by hydroxylases. These types of enzymes are either oxygenases or peroxidases, in which the source of oxygen is O2 or H2O2, respectively. Cytochrome P-450-dependent enzymes represent a common class of enzymes that carry out hydroxylation reactions. L-Carnitine is a metabolite isolated from many organisms and its biosynthesis begins with the enzymatic hydroxylation of trimethyllysine. The intermediate, 3-hydroxyl-e-(A(A(ALtrimethyl)-L-lysine, is further... 

The formation of Hyp and Hyl residues in procollagen is catalyzed by iron-containing oxygenases ( proline and lysine hydroxylase, EC 1.14.11.1/2). Ascorbate is required to maintain their function. Most of the symptoms of the vitamin C deficiency disease scurvy (see p. 368) are explained by disturbed collagen biosynthesis. 

Figure 5.S Lysine demethylation by the oxygenases of the JmJC family.

Some bacteria, e.g., Pseudomonas putidap1 degrade L-lysine with a flavin-dependent oxygenase (Eq. 18-41) to 8-aminovaleramide ... 

Although both reactions require CO2 to form a lysine carbamate on rubisco, the carboxylase reaction requires an additional CO2 to proceed. Increasing the concentration of CO2 would therefore be expected to accelerate the carboxylase reaction while not affecting the oxygenase pathway. 

All the enzymes contain ferrous iron. Ferrous ions are essential for the catalytic activity of butyrobetaine hydroxylase (259), proline-4- 254) and 3- 242, 243), hydroxylases, thymidine hydroxylase 260), lysine hydroxylase 261), trimethyllysine hydroxylase 247), thymine oxygenase 262—264), cephalosporin hydroxylase 249), and hydroxy-phenylpyruvate 265—267). In addition, the enzymes show a non-stoichio-metric requirement for ascorbic acid which is supposed to maintain the ion co-factor in the ferrous oxidation state (2, 242, 243, 254). Labelling studies with butyrobetaine hydroxylase 268), proline-4-hydroxylase 269), thymine oxygenase (270), cephalosporin hydroxylase (257) and hydroxy-phenylpyruvate hydroxylase (277) all indicate a common pattern of oxygen incorporation. One atom of oxygen becomes the new hydroxyl group while the other is located in one of the carboxylic acid groups of succinic acid. 

Ascorbic acid is required for many hydroxylase enzymes in the human body. Ascorbic acid is needed for conversion of tyrosine to the neurotransmitter dopamine and further hydroxylation to adrenaline and noradrenaline, for synthesis of carnitine from lysine, and probably for hydroxylation of steroid hormones. Ascorbate is also known to participate in hydroxylation of aromatic drugs and carcinogens via microsomal mono-oxygenase systems of Uver endoplasmic reticulum (31,32). Its role in the formation of collagen is thought to be to maintain iron in its ferrous state for an iron-dependent proline hydroxylase, or to act as a direct source of electrons for reduction of O2 (31). 

Peptidyl lysine-5-hydorxylase Ty mine-5 -oxygenase 4-Hydroxylphenylpyruvate dioxygenase... 

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