Literature summary for 1.14.13.7 extracted from

McCormick, M.S.; Lippard, S.J.
Analysis of substrate access to active sites in bacterial multicomponent monooxygenase hydroxylases: X-ray crystal structure of xenon-pressurized phenol hydroxylase from Pseudomonas sp. OX1 (2011), Biochemistry, 50, 11058-11069.

Search for more literature for 1.14.13.7

Crystallization (Commentary)

Crystallization (Comment)	Organism
computational analyses of the hydrophobic cavities in the hydroxylase alpha-subunits of phenol hydroxylase. Among the xenon-binding sites observed in phenol hydroxylase, more than 80% are localized entirely within the alpha-subunit, and 70% of those occur in the hydrophobic cavities. The hydrophobicity of a large majority of side chain residues contributing to the xenon-binding sites in the phenol hyroxylase alpha-subunit are conserved among bacterial multicomponent monooxygenases. The xenon sites delineate the path of transport of dioxygen to the diiron center during catalysis	Pseudomonas sp.

Crystallization (Comment)

Organism

computational analyses of the hydrophobic cavities in the hydroxylase alpha-subunits of phenol hydroxylase. Among the xenon-binding sites observed in phenol hydroxylase, more than 80% are localized entirely within the alpha-subunit, and 70% of those occur in the hydrophobic cavities. The hydrophobicity of a large majority of side chain residues contributing to the xenon-binding sites in the phenol hyroxylase alpha-subunit are conserved among bacterial multicomponent monooxygenases. The xenon sites delineate the path of transport of dioxygen to the diiron center during catalysis

Pseudomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	-	-
Pseudomonas sp. OX1	-	-	-

Synonyms

Synonyms	Comment	Organism
PHH	-	Pseudomonas sp.

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)