Subject(s)
Hydroxymethylglutaryl CoA Reductases/metabolism , Lovastatin/analogs & derivatives , Ubiquinone/biosynthesis , Acetates/metabolism , Cell Line , Culture Media , Fibroblasts/metabolism , Humans , Hydroxymethylglutaryl-CoA Reductase Inhibitors , Lipoproteins, LDL/pharmacology , Naphthalenes/pharmacologySubject(s)
Hydroxymethylglutaryl CoA Reductases/metabolism , Ubiquinone/biosynthesis , Cell Line , Cholesterol/biosynthesis , Fibroblasts/drug effects , Fibroblasts/enzymology , Humans , Kinetics , Lactones/metabolism , Lipoproteins, LDL/pharmacology , Mevalonic Acid/analogs & derivatives , Mevalonic Acid/metabolism , Parabens/metabolism , SkinSubject(s)
Aminobenzoates/metabolism , Mitochondria/enzymology , Transferases/metabolism , Animals , Brain/enzymology , Catecholamines/pharmacology , Escherichia coli/enzymology , Female , Hydroxybenzoates , Kidney/enzymology , Membranes/enzymology , Mitochondria, Liver/enzymology , Mitochondria, Muscle/enzymology , Myocardium/ultrastructure , Organ Specificity , Rats , Species Specificity , Spleen/enzymology , TerpenesSubject(s)
Basidiomycota/metabolism , Pigments, Biological/biosynthesis , Pyrans/metabolism , Styrenes/metabolism , Ammonia-Lyases/metabolism , Basidiomycota/drug effects , Carbon Radioisotopes , Cell-Free System , Chloramphenicol/pharmacology , Cinnamates , Coumarins , Cycloheximide/pharmacology , Darkness , Light , Lighting , Mixed Function Oxygenases/metabolism , Phenylalanine , Photochemistry , Time FactorsSubject(s)
Basidiomycota/enzymology , Mixed Function Oxygenases/metabolism , Pyrans/metabolism , Styrenes/metabolism , Ascorbic Acid/pharmacology , Basidiomycota/cytology , Chelating Agents/pharmacology , Chromatography, DEAE-Cellulose , Chromatography, Gel , Cinnamates , Cytosol/enzymology , Hydrogen-Ion Concentration , Kinetics , Mixed Function Oxygenases/isolation & purification , Molecular Weight , NAD/pharmacology , NADP/pharmacology , Oxidation-Reduction , Pigments, Biological , Structure-Activity Relationship , Subcellular Fractions/enzymologyABSTRACT
The effects of light on growth, pigmentation and the activities of enzymes involved in the deamination of phenylalanine and tyrosine and in the biosynthesis of hispidin were examined in Polyporus hispidus. Evidence is presented for the stimulation of phenylalanine ammonia-lyase activity by light. Tyrosine ammonia-lyase activity and aminotransferase activities for phenylalanine and tyrosine were higher in the dark. Tracer studies showed that conversion of cinnamate into p-coumarate is enhanced by light. p-Coumaric acid hydroxylase, catalysing the conversion of p-coumarate into caffeate, could be detected only in cultures exposed to light. These results suggest that the cinnamate pathway for the metabolism of phenylalanine, leading to hispidin synthesis, is regulated by light in P. hispidus.
Subject(s)
Ammonia-Lyases/metabolism , Basidiomycota/metabolism , Light , Pyrans/biosynthesis , Carbon Radioisotopes , Cinnamates/metabolism , Coumarins/biosynthesis , Phenylalanine/metabolism , Pyrones , Spectrophotometry, Ultraviolet , Styrenes/biosynthesis , Tyrosine/metabolismSubject(s)
Basidiomycota/enzymology , Mixed Function Oxygenases , Basidiomycota/cytology , Carbon Isotopes , Cell-Free System , Chromatography, Paper , Cinnamates , Coumarins/isolation & purification , Crystallization , Flavin-Adenine Dinucleotide , Hydrogen-Ion Concentration , Hydroxylation , Microsomes/enzymology , Mixed Function Oxygenases/isolation & purification , NADP , Subcellular Fractions/enzymologyABSTRACT
1. An enzyme responsible for the conversion of p-coumarate into caffeate was purified 97-fold from Streptomyces nigrifaciens. The enzyme had a molecular weight of 18000 as determined by Sephadex G-100 gel filtration and was homogeneous on polyacrylamide-gel electrophoresis. 2. The preparation exhibited both p-coumarate hydroxylase and caffeate oxidase activities. 3. Stoicheiometry of the reaction indicated a mono-oxygenase-mediated catalysis consuming 1mol of O(2)/mol of substrate hydroxylated. 4. NADH, NADPH, tetrahydropteroylglutamate or ascorbate act as electron donors for the reaction, ascorbate being inhibitory at higher concentrations. 5. The optimum enzyme activity was at about pH7.7 and 40 degrees C, with an activation energy of 39kJ/mol. 6. Monophenols such as p-hydroxyphenylpropionate, p-hydroxyphenylacetate, l-tyrosine and dl-p-hydroxyphenyl-lactate were also hydroxylated by the preparation, in addition to p-coumarate. 7. The enzyme was a copper protein having 0.38% copper in a bound form. 8. Thiol-group inhibitors did not affect the reaction. 9. The relationship of the enzyme to other hydroxylases is discussed.
