Chemical modification of phenol hydroxylase by ethoxyformic anhydride

Phenol hydroxylase was inactivated by ethoxyformic anhydride. Part of the inactivation was related to modification of histidyl residues. The remaining part of the inactivation is proposed to be due to the modification of a lysyl residue which, we suggest, is identical with the one previously describ...

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Published inEuropean journal of biochemistry Vol. 170; no. 1/2; pp. 351 - 356
Main Authors Sejlitz, T, Neujahr, H.Y
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 30.12.1987
Blackwell
Subjects
Analytical, structural and metabolic biochemistry
Biological and medical sciences
chemical treatment
Diethyl Pyrocarbonate - pharmacology
Enzymes and enzyme inhibitors
Formates - pharmacology
Fundamental and applied biological sciences. Psychology
Histidine
Kinetics
Lysine
Mathematics
Mixed Function Oxygenases - antagonists & inhibitors
Oxidoreductases
oxygenases
phenols
Pyridoxal Phosphate - pharmacology
Saccharomyces cerevisiae - enzymology
Spectrophotometry
Trichosporon beigelii
Yeast
Enzyme
Phenol 2-monooxygenase
Inactivation
Structure function relationship
Fungi
Chemical modification
Phenol
Histidine
Trichosporon cutaneum
Lysine
Fungi Imperfecti
Kinetics
Thallophyta
Conformation
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Summary:Phenol hydroxylase was inactivated by ethoxyformic anhydride. Part of the inactivation was related to modification of histidyl residues. The remaining part of the inactivation is proposed to be due to the modification of a lysyl residue which, we suggest, is identical with the one previously described, being essential for the binding of NADPH [Neujahr, H. Y. and Kjellén, K. G. (1980) Biochemistry 19, 4967–4972]. The overall inactivation reaction is biphasic and follows pseudo‐first‐order kinetics. Numerical analysis of kinetic data was applied to discriminate between simultaneous reactions at different sites. It is proposed that phenol hydroxylase contains two essential histidyl residues, located in or near the NADPH‐binding sites. Ethoxyformylation of the lysyl residue(s) caused tightening of the binding of phenol and perturbation of the FAD spectrum of phenol hydroxylase, similar to that caused by phenolic effectors.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1987.tb13706.x