Abstract
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].
