A novel laccase with urate oxidation activity from Lysobacter sp. T-15.
Summary of "A novel laccase with urate oxidation activity from Lysobacter sp. T-15."
A unique urate-oxidizing enzyme was identified in a bacterium, strain T-15. Based on its phylogenetic, physiological and biochemical properties, strain T-15 was deemed to be a novel species within the genus Lysobacter. The enzyme expressed in Lysobacter sp. T-15 was composed of 592 amino acids and contained 4 consensus copper-binding sites, and the recombinant enzyme was, at least in this study, speculated to have 3 Cu ions per subunit. The primary structure of the enzyme was 33% identical to Marinomonas mediterranea polyphenol oxidase, but it showed no significant similarity to any known urate oxidase. With urate as the substrate, the catalytic efficiency (k(cat)/K(m)) of recombinant enzyme was 4.0x10(2) s(-1)mM(-1), and it was not inhibited by xanthine, a strong urate oxidase inhibitor. The enzyme also showed activity toward 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid), 2,6-dimethoxyphenol and bilirubin, with catalytic efficiencies of 4.9x10(2), 1.1x10(2) and 3.6x10(3) s(-1)mM(-1), respectively. We deemed the enzyme would be a member of laccase from its broad substrate specificity. However, typical laccase and other multi-copper oxidases such as bilirubin oxidase and ascorbate oxidase seldom exhibit urate oxidation activity. These results would expand the laccase substrate range to include urate.
Institute for Biological Resources & Functions, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, Higashi 1-1-1, Tsukuba, Ibaraki 305-8566, Japan.
This article was published in the following journal.
Name: Journal of biochemistry
Medical and Biotech [MESH] Definitions
A copper-containing oxidoreductase enzyme that catalyzes the oxidation of 4-benzenediol to 4-benzosemiquinone. It also has activity towards a variety of O-quinols and P-quinols. It primarily found in FUNGI and is involved in LIGNIN degradation, pigment biosynthesis and detoxification of lignin-derived products.
An oxidation product, via XANTHINE OXIDASE, of oxypurines such as XANTHINE and HYPOXANTHINE. It is the final oxidation product of purine catabolism in humans and primates, whereas in most other mammals URATE OXIDASE further oxidizes it to ALLANTOIN.
An enzyme that catalyzes the conversion of urate and unidentified products. It is a copper protein. The initial products decompose to form allantoin. EC 220.127.116.11.
A genus of gram-negative, rod-shaped, gliding bacteria in the family XANTHOMONADACEAE. Strongly proteolytic, it is involved in lysing a variety of microorganisms.
Antagonist of urate oxidase.
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