L-Lysine Oxidase, a New Oxygenase

Itada, Nobutomo; Ichihara, Akira; Makita, Tutomu; Hayaishi, Osamu; Suda, Masami; Sasaki, Nobuji

doi:10.1093/oxfordjournals.jbchem.a127418

Cited by 20 publications

(9 citation statements)

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“…Oxygen from O2 was shown tc be incorporated into ~-amlnovaleric acid (103). The enzyme was resolved with acidified ammonium sulfate, and could be reactivated by FAD, but not by FMN or riboflavin.…”

Section: Mon0-0xygenase$mentioning

confidence: 99%

Flavoproteins

Wellner¹

1967

Annu. Rev. Biochem.

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Since the isolation of the Old Yellow Enzyme by Warburg & Christian (1 ) in 1932, the number of known flavoproteins has increased at an accel erating pace. As methods of enzyme purifi cation have become more refi ned, an increasing number of enzymes containing FAD or FMN as their prosthetic groups have been obtained in a homogeneous state, and many of these have now been crystallized. It has become apparent that these en zymes play a role in a far greater diversity of metabolic reactions than was formerly thought.The progress which has been made in techniques for studying rapid reactions in solution (2) and in the application of electron paramagnetic resonance spectroscopy (EPR) to the study of enzymatic reactions (3), as well as the availability of a number of pure flavoproteins in relatively large amounts, has allowed detailed studies of their mechanisms of action and of their chemical and physical properties to be carried out. The results have revealed the great complexity and individuality of these enzymes. After a period in which many investigators thought, perhaps wishfully, that all flavoproteins were basically similar, and that the elucidation of the mecha nism of one of these would lead to a general understanding of flavoprotein catalysis, the impression has now become prevalent that each flavoprotein is different from every other and that few generalizations are justifi ed. Nevertheless, it may perhaps still be hoped that some of these differences are not as fundamental as they appear, and that, as more knowledge about the structure and reactivity of individual flavoproteins accummulates, com mon features will emerge and generalizations will again become possible. One of the purposes of this review is to focus attention on a few selected flavoproteins, particularly some that have not been considered in recent re views on this subject. Studies on respiratory chain enzymes are reviewed by Pullman & Schatz in this volume. Much recent work on flavoproteins was reported at symposia (4-8), and was recently reviewed (9). AMINO ACID OXIDASES2Optical rotatory dispersion (ORD ).-The usefulness of optical rotato ry dispersion measurements in the study of enzyme structure and function, and particularly in the elucidation of the interactions between protein, coenzyme, substrate, and inhibitor, has been amply documented (10). The 1 The survey of literature pertaining to this review was concluded in October, 1966 . 2 For a review of earlier work, see (9a). 669 655 Annu. Rev. Biochem. 1967.36:669-690. Downloaded from www.annualreviews.org by University of Sheffield on 10/12/14. For personal use only. Quick links to online content Further ANNUAL REVIEWS 670 WELLNER application of ORD to the study of flavoproteins, however, has only recently begun. Thus, Handler, Rajagopalan & Aleman (11) have observed interesting Cotton effects exhibited by xanthine oxidase and dihydro-orotlc dehydrogenase. Howev.er, the influence of flavins on the ORD was difficult to evaluate because of the presence of strong asymmetric absorption ban...

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Section: Mon0-0xygenase$mentioning

confidence: 99%

Flavoproteins

Wellner¹

1967

Annu. Rev. Biochem.

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“…Lysine oxygenase activity was determined a t 25 "C by measurement of oxygen (1) Lysine oxygenase [30,31] ; (2) 5-aminovaleramidase [lo, 181 ; (3) 5-aminovalerate-glutamate transaminase [32] ; (4) glutarate semialdehyde dehydlrogenase [33] ; ( 5 ) glutarate degradation pathway [34--361. Recently, another pathway probably responsible for D-lySine degradation in Pseudomoms has been described [37,38] consumption with a Clark oxygen electrode YSI 4004 were usually measured a t a 40 mM lysine concentration.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Regulation of a Catabolic Pathway

Vandecasteele

Hermann

1972

European Journal of Biochemistry

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The regulation of the pathway responsible for l‐lysine degradation in Pseudomonas putida has been studied. It has been shown that l‐lysine is the actual inducer of the two first enzymes of the pathway, lysine oxygenase and 5‐aminovaleramidase. No important repression of lysine oxygenase by various carbon sources and by intermediates of the lysine degradation pathway has been found. Activation of lysine oxygenase by its substrate, lysine, has been observed. A physiological function for this phenomenom is proposed. Sodium and potassium ions are activators whereas magnesium ion, phosphate and phosphorylated compounds are inhibitors of lysine oxygenase. Citrate also is inhibitory.

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“…This enzyme was first described by Suda and his coworkers in 1960 and was shown to catalyze the conversion of L-lysine to 5-aminovaleric acid (3). It was later shown by the col-laborative effort of Suda's group and our own that at least one atom of molecular oxygen is incorporated into the product, 5-aminovaleric acid (9). Recently, we have purified and crystallized this enzyme, and have demonstrated that the primary product of the reaction is 5-aminonorvaleramide, not the free acid (21a).…”

Section: Monooxygenasesmentioning

confidence: 99%

Crystalline oxygenases of pseudomonads.

Hayaishi¹

1966

Bacteriological Reviews

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L-Lysine Oxidase, a New Oxygenase

Cited by 20 publications

References 0 publications

Flavoproteins

Flavoproteins

Regulation of a Catabolic Pathway

Crystalline oxygenases of pseudomonads.

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