Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans.
In the ascomycetous fungus Aspergillus nidulans, the expression of two inducible, contiguous or closely linked genes (qutB and qutC) which encode enzymes for quinate breakdown to protocatechuate, appears to be controlled by the product of a tightly linked third genet (qutA). The qut gene cluster locates on chromosome VIII. The catalytic steps required for this conversion are dehydrogenase, dehydroquinase, and dehydratase, and these activities are induced by the presence of quinate in a similar manner. The dehydroquinase enzyme has been purified and shown to be multimeric, consisting of 20-22 identical subunits of approximately 10,000 MW. The enzyme has a pI value of 5.84, a Km of 5 x 10(-4) M, and an amino acid composition that lacks tryptophan and cysteine. The enzyme also cross-reacts with rabbit antibodies raised against Neurospora crassa catabolic dehydroquinase.
D000429:Alcohol Oxidoreductases / Q000096:biosynthesis / Q000235:genetics*; D000596:Amino Acids / Q000032:analysis; D001233:Aspergillus nidulans / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D006836:Hydro-Lyases / Q000096:biosynthesis / Q000235:genetics; D007526:Isoelectric Point; D008970:Molecular Weight; D009154:Mutation; D011801:Quinic Acid / Q000378:metabolism*
D000596:Amino Acids; D011801:Quinic Acid; D000429:Alcohol Oxidoreductases; C022511:quinate dehydrogenase; D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase