FLAVOENZYME CATALYSIS

Flavoenzyme catalysis: substrate-competitive inhibition of D-amino acid oxidase.

In an earlier paper from this laboratory (1) there were described the characteristics of competitive inhibition resulting from the interference of certain aromatic compounds with the association of flavin adenine dinucleotide and the separated protein of n-amino acid oxidase. Included among the inhibitors were auramine, quinine, and various other quinolines and anilines. We now present our find...

Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis.

The precursor of the essential ether phospholipids is synthesized by a peroxisomal enzyme that uses a flavin cofactor to catalyze a reaction that does not alter the redox state of the substrates. The enzyme crystal structure reveals a V-shaped active site with a narrow constriction in front of the prosthetic group. Mutations causing inborn ether phospholipid deficiency, a very severe genetic di...

Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis.

Cytokinins form a diverse class of compounds that are essential for plant growth. Cytokinin dehydrogenase has a major role in the control of the levels of these plant hormones by catalysing their irreversible oxidation. The crystal structure of Zea mays cytokinin dehydrogenase displays the same two-domain topology of the flavoenzymes of the vanillyl-alcohol oxidase family but its active site ca...

New approaches for flavoenzyme applications

Dendron-based model systems for flavoenzyme activity: towards a new class of synthetic flavoenzyme.

Three generations of water-soluble flavin dendrons have been synthesized and the role dendrimer generation has on the physical and catalytic properties of these assemblies has been investigated.