Biochemical and cellular characterisation of the Plasmodium falciparum M1 alanyl aminopeptidase (PfM1AAP) and M17 leucyl aminopeptidase (PfM17LAP) [PDF]
Scientific Reports, 2021 The Plasmodium falciparum M1 alanyl aminopeptidase and M17 leucyl aminopeptidase, PfM1AAP and PfM17LAP, are potential targets for novel anti-malarial drug development.
Rency Mathew +7 more
doaj +6 more sources
Safety evaluation of the food enzyme leucyl aminopeptidase from the non‐genetically modified Lichtheimia ramosa strain AE‐PER [PDF]
EFSA JournalThe food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the non‐genetically modified Lichtheimia ramosa strain AE‐PER by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism.
EFSA Panel on Food Enzymes (FEZ) +17 more
doaj +3 more sources
Safety evaluation of an extension of use of the food enzyme leucyl aminopeptidase from the non‐genetically modified Lichtheimia ramosa strain AE‐PER [PDF]
EFSA JournalThe food enzyme leucyl aminopeptidase (AMP aminohydrolase; EC 3.4.11.1) is produced with the non‐genetically modified Lichtheimia ramosa strain AE‐PER by Amano Enzyme Inc.
EFSA Panel on Food Enzymes (FEZ) +14 more
doaj +3 more sources
Safety evaluation of a food enzyme containing leucyl aminopeptidase, oryzin and aspergillopepsin I from the non‐genetically modified Aspergillus sp. strain AE‐PR [PDF]
EFSA JournalThe food enzyme containing leucyl aminopeptidase (EC 3.4.11.1), oryzin (EC 3.4.21.63) and aspergillopepsin I (EC 3.4.23.18) activities is produced with the non‐genetically modified Aspergillus sp. strain AE‐PR by Amano Enzyme Inc.
EFSA Panel on Food Enzymes (FEZ) +17 more
doaj +3 more sources
Bacterial quorum sensing quenching activity of Lysobacter leucyl aminopeptidase acts by interacting with autoinducer synthase [PDF]
Computational and Structural Biotechnology Journal, 2021 Acyl-homoserine lactone (AHL) is the most studied autoinducer in gram-negative bacteria controlling infections of various pathogens. Quenching of AHL signaling by inhibiting AHL synthesis or AHL-receptor binding via small molecular chemicals or ...
Jinxing Liao +8 more
doaj +4 more sources
Revised safety evaluation of the food enzyme leucyl aminopeptidase from the non‐genetically modified Aspergillus sp. strain AE‐MB [PDF]
EFSA JournalThe food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the non‐genetically modified Aspergillus sp. strain AE‐MB by Amano Enzyme Inc. In a previous evaluation, the Panel concluded that the food enzyme could not be considered safe when used ...
EFSA Panel on Food Enzymes (FEZ) +15 more
doaj +3 more sources
Safety evaluation of the food enzyme leucyl aminopeptidase from non‐genetically modified Aspergillus oryzae strain NZYM‐EX [PDF]
EFSA Journal, 2023 The food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the non‐genetically modified microorganism Aspergillus oryzae strain NZYM‐EX by Novozymes A/S. The food enzyme is free from viable cells of the production organism. It is intended to be
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +26 more
doaj +2 more sources
Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families [PDF]
Marine Drugs, 2023 Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes.
Isel Pascual Alonso +8 more
doaj +2 more sources
New role for leucyl aminopeptidase in glutathione turnover. [PDF]
Biochem J, 2004 A manganese-dependent cysteinyl-glycine hydrolysing activity has been purified to electrophoretic homogeneity from bovine lens. The characterization of the purified enzyme (molecular mass of the native protein, molecular mass of the subunit and extensive primary structure analysis) allowed the unequivocal attribution of the cysteinyl-glycine ...
Cappiello M +9 more
europepmc +7 more sources
Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae [PDF]
Archives of Biological Sciences, 2004 null
Božić Nataša M. +3 more
doaj +5 more sources