EC Number |
Title |
Organism |
---|
1.21.99.1 | Accessibility of the tryptophan residues and flavin prosthetic group of beta-cyclopiazonate oxidocyclase to solvent studied by fluorescence quenching |
Penicillium cyclopium |
1.21.99.1 | beta-Cyclopiazonate oxidocyclase from Penicillium cyclopium. 3. Preliminary studies on the mechanism of action |
Penicillium cyclopium |
1.21.99.1 | beta-Cyclopiazonate oxidocyclase from Penicillium cyclopium. I. Assay methods, isolation and purification |
Penicillium cyclopium |
1.21.99.1 | beta-Cyclopiazonate oxidocyclase from Penicillium cyclopium. II. Studies on electron acceptors, inhibitors, enzyme kinetics, amino acid composition, flavin prosthetic group and other properties |
Penicillium cyclopium |
1.21.99.1 | Identification and properties of 8alpha-(N(1)-histidyl)-riboflavin: the flavin component of thiamine dehydrogenase and beta-cyclopiazonate oxidocyclase |
Penicillium cyclopium |
1.21.99.1 | Identification and properties of the covalently bound flavin of beta-cyclopiazonate oxidocyclase |
Penicillium cyclopium |
1.21.99.1 | Structural elucidation and properties of 8alpha-(N1-histidyl)riboflavin: the flavin component of thiamine dehydrogenase and beta-cyclopiazonate oxidocyclase |
Penicillium cyclopium |
1.21.99.1 | The binding of indole derivatives by borohydride-reduced beta-cyclopiazonate oxidocyclase |
Penicillium cyclopium |
1.21.99.1 | The covalently bound flavin prosthetic group of beta-cyclopiazonate oxidocyclase |
Penicillium cyclopium |
1.21.99.1 | The excreted beta-cyclopiazonate oxidocyclase isoenzymes from Penicillium clyclopium. II. Evidence for an ping-pong bi-bi mechanism from substrate inhibition studies |
Penicillium cyclopium |