Phenol Hydroxylase from Yeast. Sulfhydryl Groups in Phenol Hydroxylase from Trichosporon cutaneum
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چکیده
منابع مشابه
Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strain.
The phenol-degrading strain Trichosporon cutaneum R57 utilizes various aromatic and aliphatic compounds as a sole carbon and energy source. The intracellular activities of phenol hydroxylase [EC 1.14.13.7] of a Trichosporon cutaneum R57 strain grown on phenol (0.5 g/l) were measured. Different toxic phenol derivatives (cresols, nitrophenols and hydroxyphenols) were used as substrates in the rea...
متن کاملUptake of phenol by Trichosporon cutaneum.
The soil yeast Trichosporon cutaneum, which is distinguished by having a strictly oxidative metabolism, can be induced to utilize phenol as a sole carbon source. The present paper shows that such phenol-induced cells contain a specific, energy-dependent uptake system for phenol. Phenol uptake is not directly linked to its o-hydroxylation inside the cell, the first step of phenol metabolism. The...
متن کاملProperties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum.
Anthranilate hydroxylase was purified from the yeast Trichosporon cutaneum. This enzyme is a simple flavoprotein which apparently does not require any additional cofactor for the conversion of anthranilate to 2,3-dihydroxybenzoate. Anthranilate hydroxylase has Mr of approximately 95,000, with subunit Mr of 50,000; it contains 2 mol of FAD/mol of enzyme. A number of compounds in addition to anth...
متن کاملProperties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum.
Salicylate hydroxylase (salicylate 1-monooxygenase, EC 1.14.13.1) was purified from the soil yeast Trichosporon cutaneum. The enzyme contained flavin adenine dinucleotide and was monomeric, with a molecular weight of 45,300. In addition to salicylate, the four isomeric dihydroxybenzoates having one hydroxyl adjacent to carboxyl in the benzene nucleus were oxidatively decarboxylated without form...
متن کاملIsolation of cytoplasmic NADPH-dependent phenol hydroxylase and catechol-1,2-dioxygenase from Candida tropicalis yeast
The efficiencies of NADPH-dependent phenol hydroxylase (EC 1.14.13.7) and catechol 1,2-dioxygenase (EC.1.13.11.1) in biodegradation of phenol in the cytosolic fraction isolated from yeast Candida tropicalis were investigated. Enzymatic activities of both NADPH-dependent phenol hydroxylase and catechol 1,2-dioxygenase were detected in the cytosolic fraction of C. tropicalis grown on medium conta...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1975
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1975.tb02381.x