Dienelactone hydrolase from Pseudomonas cepacia.
Dienelactone hydrolases have previously been shown to play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. Recently, the enzymes induced in 4-fluorobenzoate-utilizing bacteria have been classified into three groups on the basis of their specificity towards cis- and trans-dienelactone. The dienelactone hydrolase and the 3-oxoadipate enol-lactone hydrolase from Pseudomonas cepacia have now been purified to apparent homogeneity and characterized with respect to molecular mass and amino acid composition. The dienelactone hydrolase has a distinct preference for cis-dienelactone and did not convert the trans isomer or muconolactone, 3-oxoadipate enol-lactone, or 4-fluoromuconolactone to a significant extent. In properties like amino acid composition, pH optimum of activity, and lack of inhibition by p-chloromercuribenzoate, the P. cepacia dienelactone hydrolase differed substantially from 3-oxoadipate enol-lactone hydrolases and other dienelactone hydrolases.
Schlömann
M
M
Institut für Mikrobiologie, Universität Stuttgart, Germany.
Ngai
K L
KL
Ornston
L N
LN
Knackmuss
H J
HJ
D000595:Amino Acid Sequence; D016956:Burkholderia cepacia / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity
D002265:Carboxylic Ester Hydrolases; C021927:3-oxoadipate enol-lactonase; C046130:carboxymethylenebutenolidase