Ureidoglycollate lyase, a new metalloenzyme of peroxisomal urate degradation in marine fish liver.

Y. Takada, T. Noguchi

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Ureidoglycollate lyase (UGL, EC 4.3.2.3), which catalyses the degradation of S(-)-ureidoglycollate to urea and glyoxylate, was found in the peroxisomes of marine fish (sardine and mackerel) liver. The enzyme highly purified from sardine liver had an Mr of about 121,000, with two identical subunits. When UGL was purified in the presence of 1 mM-EDTA, a much less active form was obtained. It was markedly activated by bivalent metal ions, particularly by Mn2+. The Mn2+-activated enzyme remained active when free Mn2+ was removed by gel filtration on Sephadex G-50, suggesting that UGL may be a metalloenzyme and the activation resulted from the binding of Mn2+ to the apoenzyme. UGL was found to be essential in peroxisomal urate degradation, since allantoate, the intermediate of urate catabolism, was found to be degraded to urea and glyoxylate in a two-step reaction catalysed by allantoicase (EC 3.5.1.5) and UGL via S(-)-ureidoglycollate as an intermediate in fish liver peroxisomes, but not in a one-step reaction as previously believed.

Original languageEnglish
Pages (from-to)391-397
Number of pages7
JournalBiochemical Journal
Volume235
Issue number2
Publication statusPublished - Apr 15 1986
Externally publishedYes

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ureidoglycollate lyase
Uric Acid
Liver
Fish
Fishes
Peroxisomes
allantoicase
Degradation
Urea
Apoenzymes
Perciformes
Enzymes
Edetic Acid
Gel Chromatography
Metal ions
Gels
Metals
Chemical activation
Ions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ureidoglycollate lyase, a new metalloenzyme of peroxisomal urate degradation in marine fish liver. / Takada, Y.; Noguchi, T.

In: Biochemical Journal, Vol. 235, No. 2, 15.04.1986, p. 391-397.

Research output: Contribution to journalArticle

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