(Q27759050)

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The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

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The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis (English)

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crystal structure

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object named as

Y Lindqvist

4

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Gunter Schneider

object named as

G Schneider

3

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author name string

C Enroth

1

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H Neujahr

2

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publication date

15 May 1998

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6

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605-17

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5

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Degradation of phenols by intact cells and cell-free preparations of Trichosporon cutaneum

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Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum

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Growth and enzyme synthesis during continuous culture of Trichosporon cutaneum on phenol

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Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli

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Phenol hydroxylase from yeast. A model for phenol binding and an improved purification procedure

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A fermentor culture for production of recombinant phenol hydroxylase.

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In situ and in vitro kinetics of phenol hydroxylase.

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Thiol- and pH-modulated slow conformational changes and cooperativity of phenol-binding sites in phenol hydroxylase

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Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding

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Crystal structure of p-hydroxybenzoate hydroxylase

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Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes

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Crystallization and Preliminary X-ray Analysis of Phenol Hydroxylase from Trichosporon cutaneum

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Absolute stereochemistry of flavins in enzyme-catalyzed reactions

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Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton [...]

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Solvent content of protein crystals

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Identifiers

10.1016/S0969-2126(98)00062-8

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