L lysine oxidase

In an original application, Yasuda et al have used both l-AAO and d-AAO, and L-lysine oxidase to oxidize o ,Ci -diamino acids. The reactions produce the expected a-keto w-amino acid products, but these then spontaneously cyclize to form cyclic a-imino acids. These compounds are then substrates for the authors recently discovered A methyl amino acid dehydrogenase (NMAADH) from Pseudomonas putida, producing the pure L-cyclic amino acid (Scheme 5). 

Scheme 2.16 Synthesis of cyclic amino acid (R)-40 by combined use of L-lysine oxidase and NMAADH.

D-Aspartate oxidase L-Amino-acid oxidase D-Amino-acid oxidase Amine oxidase (flavin-containing) Amine oxidase (copper-containing) D-Glutamate oxidase Ethanolamine oxidase Putrescine oxidase L-Glutamate oxidase L-Lysine oxidase... 

More recently, L-lysine oxidase was shown to catalyze incorporation of atmospheric oxygen. The over-all reaction is quite similar to that catalyzed by lactic oxidative decarboxylase and is shown below (Itada et al., 1961) (Eq. 27). 

L-Lysine oxidase is a possible candidate for a nonmetallic catalyst. No specific absorbance, except that of protein (275 m/i), was detected in the visible and ultraviolet regions (Suda, see Hayaishi 1958). Another... 

L-Lysine is converted by an enzyme from a strain of Pseudomonas into y-aminovalerianic acid, NH3, and COg. The rate of incorporation of in dry matter is fairly important. These results point to the frequent occurrence of reactions such as (91) and many others similar and unknown. In the L-lysine oxidase experiments oxygen consumption cannot be affected by crystalline catalase. Methylene blue, triphenyltetrazolium chloride, and 2,6-dichlorophenolindolephenol cannot replace oxygen. 

Preuschoff F., Spohn U., Weber E., Unverhau K., Mohr K.H., Chemiluminometric L-lysine determination with immobilized lysine oxidase by flow-injection analysis, Anal. Chim. Acta 1993 280 185-189. 

L-Pipecolic acid, a key component of many antibiotic and anticancer biomolecules, serves as an important chiral pharmaceutical intermediate. We have developed an enzyme-coupled system consisting of zl -piperidine-2-carboxylate reductase (Pip2C) from Pseudomonas putida, glucose dehydrogenase (GDH) from Bacillus subtilis, and L-lysine a-oxidase from Trichoderma viride, affording L-pipecolic acid from L-lysine in high yield with an excellent enantioselectivity (Figure 10.2). ... 

L-lysine a-oxidase from T. viride (Seikagaku Corporation, 30 units) catalase from bovine liver (Sigma-Aldrich, 500 units)... 

The same group has exploited this interesting dehydrogenase for the synthesis of cyclic amino acids from linear precursors by developing a one-pot, two-enzyme system (Scheme 2.16). t-Lysine oxidase or L- or d-AAO were initially used to... 

Biosensors are also available for glucose, lactate, alcohol, sucrose, galactose, uric acid, alpha amylase, choline, and L-lysine. All are amperometric sensors based on O2 consumption or H2O2 production in conjunction with the turnover of an enzyme in the presence of substrate. In the case of glucose oxidase reaction, the normal biological reaction is ... 

L-Lysine L-Lysine a-oxidase Milk, pasta Nutritional value assessment of food processing techniques... 

Kelly et al. [68] L-Lysine Protein samples from milk and pasta L-Lysine a-oxidase/with BSA and glutaraldehyde Ruthenium/rhodium coated glassy carbon electrode covered with 1,2-diaminobenzene polymer/ + 100 mV vs. an Ag/AgCl ... 

RL Hanson, KS Bembenek, RN Patel, LJ Szarka. Transformation of N-e-CBZ-L-lysine to CBZ-L-oxylysine using L-amino acid oxidase from Providencia alcalifa-ciens and L-2-hydroxy-isocaproate dehydrogenase from Lactobacillus confusus. Appl Microbiol Biotechnol 37 599-603, 1992. 

L-Lysine and L-arginine are determined in a rapid fashion by using a bienzyme-immobilized system, decarboxylase-diamine oxidase ... 

Recently, selective oxidases for L-lysine (EC 1.4.3.-) (Romette et al., 1983) and L-glutamate (EC 1.4.3.11) have been employed in enzyme electrodes. Wollenberger et al. (1989) developed a sensor based on glutamate oxidase from Streptomyces endus, which permits selective measurement of glutamic acid between 1 pmol/1 and 1 mmol/1 with a sample frequency of 120/h. In contrast, a sensor using an analogous... 

Although the activity of purified N. europaea cytochrome c oxidase to catalyze the oxidation of N. europaea ferrocytochrome c-552 is fairly low in vitro, it is much stimulated by addition of poly-L-lysine. For example, one molecule of the oxidase catalyzes the oxidation of nine molecules of ferrocytochrome c-552 per second in 40 mM phosphate buffer, pH 6.0, while the activity is raised up to the oxidation of 64 molecules of the ferrocytochrome c per second on addition of 5 pM poly-L-lysine (Yamazaki et al., 1988). Therefore, poly-L-lysine or similar compounds may occur in the plasma membrane of the bacterium, or some similar microenvironments caused by the presence of poly-L-lysine may occur in vivo. 

The absolute configuration of 21 was established by two methods. First, 21 was converted to 5-phthalimido[5-2H]valerate by the use of chemical and enzymic methods and shown to have the same optical rotatory properties as those of authentic (5/ )-5-phthalimido[5- H]valerate produced from L-glutamate by an established stereochemical route. Second, 21 was converted to [l- H]cadavarine with L-lysine decarboxylase, followed by treatment with diamine oxidase to form pelletierine. Retention of all of the deuterium in the pelletierine demonstrated that the deuterium must be in the pro-(R) position, since the oxidase reaction is known to labilize hydrogen at the pro-(S) position [Eq. (51)] ... 

In further consideration of the biosynthesis of the piperidine alkaloids the question of the significance of the incorporation of cadaverine must be answered. Accordingly further research has been directed to this point and it has been shown that cadaverine is a normal component of S. acre, that it is a specific precursor of sedamine (20), and that it is formed from lysine at the same time as sedamine. It follows then that any scheme for the biosynthesis of the piperidine alkaloids which does not accommodate cadaverine as a normal component is unrealistic An eminently reasonable hypothesis which fits all the evidence is shown in Scheme 1 it was anticipated in last year s Report. For those alkaloids derived from lysine without the intervention of a symmetrical intermediate, cadaverine formed by decarboxylation of lysine must remain enzyme-bound and therefore unsymmetrical. Exogenous cadaverine enters the pathway at this point by absorption on to the enzyme to give (29). In order to explain the incorporation of lysine into some alkaloids by way of a symmetrization step it is necessary only to postulate equilibration of bound with unbound cadaverine. The proposal that pyridoxal phosphate is involved in this pathway is more than mechanistically attractive, for L-lysinedecarboxylase (EC 4.1.1.18, L-lysine carboxy-lyase) and diamine oxidase [EC 1.4.3.6, diamine oxygen oxidoreductase (deaminating)], the two enzymes whose participation in the conversion of lysine into A -piperideine (30) is likely, both require pyridoxal phosphate as a co-factor. 

An estimation of the amount of amino acid production and the production methods are shown ia Table 11. About 340,000 t/yr of L-glutamic acid, principally as its monosodium salt, are manufactured in the world, about 85% in the Asian area. The demand for DL-methionine and L-lysine as feed supplements varies considerably depending on such factors as the soybean harvest in the United States and the anchovy catch in Pern. Because of the actions of d-amino acid oxidase and L-amino acid transaminase in the animal body (156), the D-form of methionine is as equally nutritive as the L-forni, so that DL-methioiiine which is inexpensively produced by chemical synthesis is primarily used as a feed supplement. In the United States the methionine hydroxy analogue is partially used in place of methionine. The consumption of L-lysine has increased in recent years. The world consumption tripled from 35,000 t in 1982 to 100,000 t in 1987 (214). Current world consumption of L-tryptophan and L-threonine are several tens to hundreds of tons. The demand for L-phenylalanine as the raw material for the s57nthesis of aspartame has been increasing markedly. 

---