A new enzyme: long acyl aminoacylase from Pseudomonas diminuta.
A new enzyme which hydrolyzes N-long chain acyl glutamic acid was found in cell-free extracts of Pseudomonas diminuta. Two active fractions (long acyl aminoacylase I and II) were separated by DEAE-cellulose column chromatography. The long acyl aminoacylase I was purified about 650-fold, and the purified preparation was electrophoretically homogeneous. The molecular weight was estimated to be 300,000 by gel filtration. The enzyme was unique in its substrate specificity. It hydrolyzed only N-long acyl glutamic acid and could not react with other N-acyl amino acids. Lauroyl (C12)-, myristoyl (C14)-, and palmitoyl (C16)- glutamic acid were good substrates, but acetyl glutamic acid was not hydrolyzed. Therefore this enzyme is considered to be a new acylase which is specific for N-long chain acyl glutamic acid, and it is designated as N-long acyl glutamic acid amidohydrolase [EC 3.5.1 group].
D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
D000581:Amidohydrolases; C035333:acyl glutamic acid amidohydrolase