Isolation and characterization of N-long chain acyl aminoacylase from Pseudomonas diminuta.
N-Long chain acyl aminoacylase II (Enzyme II) catalyzing the hydrolysis of N-long chain acyl amino acids was purified about 2,000-fold from the cell extracts of Pseudomonas diminuta with 1.8% of activity yield. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis and the molecular weight was 220,000. Enzyme II differed from N-long chain acyl aminoacylase I (Enzyme I) in molecular weight, in substrate specificity, and in behavior toward temperature and pH. Enzyme II showed broader substrate specificity than Enzyme I and catalyzed the hydrolysis of lipoamino acids containing various amino acid residues, although Enzyme I was almost specific to the lipoamino acids containing L-glutamate. The extent of hydrolysis by Enzyme II reaction varied depending on the kinds of lipoamino acids and were: 100% for palmitoyl-L-glutamate, 91% for myristoyl-L-glutamate, 85% for lauroyl-L-glutamate, 54% for lauroyl-L-aspartate, 28% for stearoyl-L-glutamate and 17.5% for lauroyl-glycine.
D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D013816:Thermodynamics
D007527:Isoenzymes; D000581:Amidohydrolases; C043812:long-chain-fatty-acyl-glutamate deacylase