Similar structures in gamma-carboxymuconolactone decarboxylase and beta-ketoadipate succinyl coenzyme A transferase.
gamma-Carboxymuconolactone decarboxylase (EC 4.1.1.44) and beta-ketoadipate succinyl coenzyme A transferase (EC 2.8.3.6) mediate different steps in the beta-ketoadipate pathway. Antisera prepared against the Pseudomonas putida transferase cross-reacted immunologically with the decarboxylase from the same organism. The transferase is formed by association of two nonidentical protein subunits. The NH2-terminal amino acid sequences of the two nonidentical transferase subunits resembled each other and also were similar to the NH2-terminal amino acid sequence of the decarboxylase.
D000150:Acinetobacter / Q000201:enzymology; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005075:Biological Evolution; D002262:Carboxy-Lyases / Q000032:analysis / Q000276:immunology; D015256:Coenzyme A-Transferases; D000939:Epitopes; D011233:Precipitin Tests; D011549:Pseudomonas / Q000201:enzymology*; D013466:Sulfurtransferases / Q000032:analysis* / Q000276:immunology
D000596:Amino Acids; D000939:Epitopes; D013466:Sulfurtransferases; D015256:Coenzyme A-Transferases; C028573:3-oxoadipate CoA-transferase; D002262:Carboxy-Lyases; C019832:4-carboxymuconolactone decarboxylase