Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea-ochracea.
Sulochrin oxidase is a blue copper-containing glycoenzyme that catalyzes a stereospecific formation of bisdechlorogeodin from sulochrin. The enzyme has been isolated from Penicillium frequentans and Oospora sulphurea-ochracea which catalyzes the formation of (+)-form and (-)-form of bisdechlorogeodin respectively. The Penicillium enzyme has a molecular weight of 157,000 and contains 19.5% of carbohydrates. Amino acid and carbohydrate compositions are given. The enzyme has probably a dimeric structure containing 6 Cu-atoms. Apparent Km-values of various substrates are presented. The Oospora enzyme has a molecular weight of 128,000 and except for its stereospecificity its properties are very similar to those of the Penicillium enzyme.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001572:Benzofurans / Q000096:biosynthesis*; D002241:Carbohydrates / Q000032:analysis; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D013045:Species Specificity; D013141:Spiro Compounds; D013379:Substrate Specificity
D000596:Amino Acids; D001572:Benzofurans; D002241:Carbohydrates; D013141:Spiro Compounds; C035076:bisdechlorogeodin; D000429:Alcohol Oxidoreductases; C035077:sulochrin oxidase