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

Y. Takada; N. Tsukiji

doi:10.1128/jb.169.5.2284-2286.1987

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

Y. Takada
, N. Tsukiji

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2284-2286
Number of pages	3
Journal	Journal of Bacteriology
Volume	169
Issue number	5
DOIs	https://doi.org/10.1128/jb.169.5.2284-2286.1987
Publication status	Published - 1987
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Microbiology

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10.1128/jb.169.5.2284-2286.1987

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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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AU - Takada, Y.

AU - Tsukiji, N.

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Y1 - 1987

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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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U2 - 10.1128/jb.169.5.2284-2286.1987

DO - 10.1128/jb.169.5.2284-2286.1987

M3 - Article

C2 - 3571167

AN - SCOPUS:0023265937

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

Abstract

ASJC Scopus subject areas

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