prolyl aminopeptidase activity

Trait evidence (3)

• https://iubmb.qmul.ac.uk/enzyme/EC3/4/11/5.html

  <b>Reaction:</b> Release of N-terminal proline from a peptide

  The NC-IUBMB EC 3.4.11.5 entry accepts prolyl aminopeptidase, gives the N-terminal-proline release reaction, and records proline aminopeptidase, Pro-X aminopeptidase, and proline iminopeptidase as other names.

• DOI:10.1111/j.1365-2958.1993.tb01249.x

  Proline iminopeptidase (Pip) is a hydrolase elaborated by virtually all strains of Neisseria gonorrhoeae that selectively removes N-terminal proline residues from peptides.

  Albertson and Koomey cloned the gonococcal pip gene and confirmed that the encoded enzyme can release biologically active proline from peptides.

• DOI:10.1099/ijsem.0.006017

  enzymatic activities are present for: α-galactosidase, N-acetyl-β-glucosaminidase, arginine arylamidase, proline arylamidase, leucyl glycine arylamidase, phenylalanine arylamidase, leucine arylamidase, tyrosine arylamidase, alanine arylamidase, glycine arylamidase, histidine arylamidase, glutamyl glutamic acid arylamidase, serine arylamidase, valine arylamidase, cysteine arylamidase, esterase, esterase lipase, alpha-chymotrypsin

  Srinivasan et al. listed proline arylamidase among enzymatic activities present in the Amygdalobacter indicium species description, supporting the API proline arylamidase row as a directly assayed bacterial enzyme-activity phenotype.