Results 11 to 20 of about 1,860 (145)

Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae [PDF]

Archives of Biological Sciences, 2004
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Božić Nataša M., Vujčić Zoran M., Nenadović Vera A., Ivanović J.   +3 more
doaj   +5 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, Lazzarotti A, Buono F, Scaloni A, D'Ambrosio C, Amodeo P, Méndez BL, Pelosi P, Del Corso A, Mura U.   +9 more
europepmc   +7 more sources

Safety evaluation of the food enzyme leucyl aminopeptidase from the genetically modified Aspergillus oryzae strain NZYM‐BU [PDF]

EFSA Journal
The food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the genetically modified Aspergillus oryzae strain NZYM‐BU by Novozymes A/S. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Magdalena Andryszkiewicz, Erik Boinowitz, Boet Glandorf, Natalia Kovalkovicova, Giulio Di Piazza, Yi Liu, Simone Lunardi, Daniele Cavanna, Yrjö Roos, Andrew Chesson   +26 more
doaj   +2 more sources

Safety evaluation of the food enzyme leucyl aminopeptidase from the non‐genetically modified Aspergillus sp. strain AE‐MB [PDF]

EFSA Journal
The 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. The food enzyme is considered free from viable cells of the production organism. It is intended to be used
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Yrjö Roos, Jaime Aguilera, Magdalena Andryszkiewicz, Daniele Cavanna, Cristina Fernàndez‐Fraguas, Simone Lunardi, Yi Liu, Giulio diPiazza, Karin Norby, Elsa Nielsen, Andrew Chesson   +27 more
doaj   +2 more sources

Aminopeptidase M17 in bacteria: insights into structure, function, and potential as a drug target [PDF]

Journal of Bacteriology
Leucyl-aminopeptidase (LAP) is a type of protease that targets peptides and the nitrogen terminus of protein molecules, playing a key role in the removal of amino acids.
Hussam Askar, Shengli Chen, Huafang Hao, Xiangrui Jin, Ahmed Adel Baz, Shimei Lan, Zhangcheng Li, Yuefeng Chu   +7 more
doaj   +2 more sources

Identification and Validation of Compounds Targeting <i>Leishmania major</i> Leucyl-Aminopeptidase M17. [PDF]

ACS Infect Dis
داء الليشمانيات هو مرض استوائي مهمل ؛ لا يوجد حاليًا لقاح ويعتمد العلاج على حفنة من الأدوية التي تعاني من مشاكل متعددة بما في ذلك السمية والمقاومة. هناك حاجة ماسة لتطوير علاجات جديدة مناسبة للغرض، مع تقليل السمية واستهداف آليات جديدة للتغلب على المقاومة.
Aguado ME, Carvalho S, Valdés-Tresanco ME, Lin, Padilla-Mejia N, Corpas-Lopez V, Tesařová M, Lukeš J, Gray D, González-Bacerio J, Wyllie S, Field MC.   +11 more
europepmc   +5 more sources

Expansion and functional diversification of a leucyl aminopeptidase family that encodes the major protein constituents of Drosophila sperm [PDF]

BMC Genomics, 2011
Background The evolutionary diversification of gene families through gene creation (and loss) is a dynamic process believed to be critical to the evolution of functional novelty.
Karr Timothy L, Wilkin Elaine C, Dorus Steve   +2 more
doaj   +2 more sources

Revised safety evaluation of the food enzyme leucyl aminopeptidase from the non‐genetically modified Aspergillus sp. strain AE‐MB [PDF]

EFSA Journal
The 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), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Monika Sramkova, Henk Van Loveren, Laurence Vernis, Eleonora Marini, Yi Liu   +15 more
doaj   +2 more sources

Leucyl and Cystinyl Aminopeptidase as a Prognostic-Related Biomarker in OV Correlating with Immune Infiltrates

Pharmacogenomics and Personalized Medicine, 2023
Qian Ma,1,* Lei Chang,2,* Wenwen Wang,2,* Lingyi Che,1 Xiaoqin Song,3 Gailing Li,2 Ying Zhang,2 Yibing Chen,1 Zhuoyu Gu,4 Xin Ge5 1Genetics and Prenatal Diagnosis Center, First Affiliated Hospital, Zhengzhou University, Zhengzhou, 450052 ...
Ma Q, Chang L, Wang W, Che L, Song X, Li G, Zhang Y, Chen Y, Gu Z, Ge X   +9 more
doaj   +3 more sources

Biomarkers of oxidative stress, biochemical changes, and the activity of lysosomal enzymes in the livers of rainbow trout (Oncorhynchus mykiss Walbaum) vaccinated against yersiniosis before a Yersinia ruckeri challenge [PDF]

Journal of Veterinary Research
This study aimed to evaluate biomarkers of oxidative stress (2-thiobarbituric acid reactive substances, aldehyde and ketone derivatives of oxidatively modified proteins and total antioxidant capacity), the activity of antioxidant enzymes (superoxide ...
Kurhaluk Natalia, Grudniewska Joanna, Pękala-Safińska Agnieszka, Pajdak-Czaus Joanna, Terech-Majewska Elżbieta, Platt-Samoraj Aleksandra, Tkaczenko Halina   +6 more
doaj   +2 more sources