Literature summary for 1.14.13.7 extracted from

Xu, D.; Ballou, D.P.; Massey, V.
Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met (2001), Biochemistry, 40, 12369-12378.

Search for more literature for 1.14.13.7

Cloned(Commentary)

Cloned (Comment)	Organism
-	Cutaneotrichosporon cutaneum

Protein Variants

Protein Variants	Comment	Organism
D54N	slower reaction than wild type enzyme, higher dissociation constant for binding of phenol than wild type enzyme	Cutaneotrichosporon cutaneum
R281M	slower reaction than wild type enzyme, binds the FAD cofactor more weakly than wild type enzyme	Cutaneotrichosporon cutaneum
Y298F	binds phenol more weakly than wild type enzyme	Cutaneotrichosporon cutaneum

Organism

Organism	UniProt	Comment	Textmining
Cutaneotrichosporon cutaneum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Cutaneotrichosporon cutaneum

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Release 2023.1 (January 2023)