Peroxisomal localization and activation by bivalent metal ions of ureidoglycolate lyase, the enzyme involved in urate degradation in Candida tropicalis

Y. Takada; N. Tsukiji

Peroxisomal localization and activation by bivalent metal ions of ureidoglycolate lyase, the enzyme involved in urate degradation in Candida tropicalis

Y. Takada, N. Tsukiji

研究成果: 雜誌貢獻 › 文章 › 同行評審

摘要

Ureidoglycolate lyase (EC 4.3.2.3) was found only in the peroxisomes in urate-induced Candida tropicalis. The enzyme was markedly activated by the bivalent metal ions Mn²⁺, Fe²⁺, and Ni²⁺. The activation by Mn²⁺ was suggested to be the result of its binding to the apoenzyme.

原文	英語
頁（從 - 到）	2284-2286
頁數	3
期刊	Journal of Bacteriology
卷	169
發行號	5
出版狀態	已發佈 - 1987
對外發佈	是

ASJC Scopus subject areas

應用微生物與生物技術
免疫學

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abstract = "Ureidoglycolate lyase (EC 4.3.2.3) was found only in the peroxisomes in urate-induced Candida tropicalis. The enzyme was markedly activated by the bivalent metal ions Mn2+, Fe2+, and Ni2+. The activation by Mn2+ was suggested to be the result of its binding to the apoenzyme.",

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N2 - Ureidoglycolate lyase (EC 4.3.2.3) was found only in the peroxisomes in urate-induced Candida tropicalis. The enzyme was markedly activated by the bivalent metal ions Mn2+, Fe2+, and Ni2+. The activation by Mn2+ was suggested to be the result of its binding to the apoenzyme.

AB - Ureidoglycolate lyase (EC 4.3.2.3) was found only in the peroxisomes in urate-induced Candida tropicalis. The enzyme was markedly activated by the bivalent metal ions Mn2+, Fe2+, and Ni2+. The activation by Mn2+ was suggested to be the result of its binding to the apoenzyme.

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Peroxisomal localization and activation by bivalent metal ions of ureidoglycolate lyase, the enzyme involved in urate degradation in Candida tropicalis

摘要

ASJC Scopus subject areas

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指紋

引用此