A new type of muconate cycloisomerase from Rhodococcus rhodochrous strain 89.
Muconate cycloisomerase (MCI) was purified from Rhodococcus rhodochrous 89 grown on phenol. The enzyme appears to contain two different type subunits with molecular masses 35.5 and 37 kD. The N-terminal amino acid sequence of both subunits showed more similarity to corresponding enzymes from gram-negative bacteria than to one from Rhodococcus opacus 1CP. MCI from R. rhodochrous 89, like analogous enzymes from gram-negative bacteria, can convert 2-chloromuconate (2-CM) with the formation of both, 2- and 5-chloromuconolactones (CML) as intermediates. Nevertheless, its unique ability to convert 5-CML to cis- but not to trans-dienelactone sets it apart from all known chloromuconate cycloisomerases from gram-negative and gram-positive bacteria.
Solyanikova
I P
IP
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Schlömann
M
M
Golovleva
L A
LA
D000272:Adipates / Q000378:metabolism*; D000595:Amino Acid Sequence; D019753:Intramolecular Lyases / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D021122:Protein Subunits; D012240:Rhodococcus / Q000201:enzymology*; D013011:Sorbic Acid / Q000031:analogs & derivatives* / Q000378:metabolism*
D000272:Adipates; D021122:Protein Subunits; C088140:2-chloromuconic acid; D019753:Intramolecular Lyases; C021811:muconate cycloisomerase; D013011:Sorbic Acid