Aminopeptidases

The influence of α-aminophosphonic acids on the activity of aminopeptidase from barley seeds—an approach to determine the enzyme specificity

“…They are necessary for proper functioning of eukaryotic and prokaryotic cells, but often are also important factors in various pathological states and diseases such as: malaria, cancer, diabetes, HIV, cataracts, angiogenesis, hypertension, systemic lupus (Hooper and Lendeckel 2004;Sanderink et al 1988;Sanz 2007;Jankiewicz and Bielawski 2003;Pulido-Cejudo et al 1997;Taylor et al 1982;Sharma et al 1996;Inokuma et al 1999;Umezawa 1980;Pretlow et al 1994;Mathe 1991).…”

Crystal Structure of the Leucine Aminopeptidase from Pseudomonas putida Reveals the Molecular Basis for its Enantioselectivity and Broad Substrate Specificity

“…1,2 Aminopeptidases have attracted additional interest due to their applicability for the production of peptides and amino acids used in the food, agrochemical and pharmaceutical industries. [3][4][5][6] An example of such an industrial enzyme is the leucine aminopeptidase from Pseudomonas putida ATCC 12633 (ppLAP), which has a longstanding use as a whole-cell biocatalyst for the enantioselective hydrolysis and enzymatic resolution of a broad range of DL-amino acid amide racemates. 7,8 PpLAP is a member of the M17 family of di-zinc-dependent leucine aminopeptidases (LAPs; EC 3.4.11.1 and EC 3.4.11.10), 9,10 which also includes the well studied LAPs from bovine lens (blLAP) and Escherichia coli (ecLAP, also known as PepA).…”

APN1 is a functional receptor of Cry1Ac but not Cry2Ab in Helicoverpa zea

“…Aminopeptidases N (APNs) are a class of broad-specificity metalloaminopeptidases that sequentially and preferentially remove neutral amino acids from the N-terminus of a range of peptides in microorganisms, plants and animals 1 . They share two conserved signature motifs: a catalytic zinc binding/gluzincin motif HEXXH-(X18)-E and an N-terminal amino acid substrate-binding exopeptidase motif GXMEN 2 3 .…”

“…In the catalytic HEXXH-(X18)-E motif, the two histidine residues and the distant gluatamic acid residue constitute zinc ligands, whereas the gluatamic acid residue between the two histidine residues and zinc ion catalyze the sequential release of N-terminal neutral amino acids 3 . By virtue of the two conserved motifs, APNs efficiently retrieve amino acids from dietary proteins and endogenous proteins degraded during protein turnover and thus play important roles in nutrition, protein maturation, peptide hormone level regulation, stress response, cell signaling, cell cycle control, and cellular processes involved in health and diseases 1 4 .…”