Purification and characterization of two muconate cycloisomerase isozymes from aniline-assimilating Frateuria species ANA-18.
Two muconate cycloisomerases (MC I and MC II, EC 5.5.1.1) were purified to homogeneity from an aniline-grown Frateuria sp. ANA-18. MC I and MC II were similar in molecular mass, optimal pH, and pH stability but different in thermostability, and some other enzymatic properties. NH2-terminal amino acid sequences were different between the two isozymes, indicated that these are encoded by different genes. Different inducible production of MC I and MC II suggested that two catechol branches involved in the beta-ketoadipate pathway function in Frateuria sp. ANA-18.
Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Japan.
S
S
Murakami
J
J
Takemoto
A
A
Takashima
R
R
Shinke
K
K
Aoki
D000595:Amino Acid Sequence; D000814:Aniline Compounds / Q000378:metabolism*; D050548:Catechol 1,2-Dioxygenase; D003470:Culture Media; D049308:Dioxygenases; D004790:Enzyme Induction; D004795:Enzyme Stability; D016946:Gram-Negative Aerobic Rods and Cocci / Q000201:enzymology / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D019753:Intramolecular Lyases / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010105:Oxygenases / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D000814:Aniline Compounds; D003470:Culture Media; D007527:Isoenzymes; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; D019753:Intramolecular Lyases; C021811:muconate cycloisomerase; C023650:aniline