Results 31 to 40 of about 4,894 (170)

How innate immunity proteins kill bacteria and why they are not prone to resistance [PDF]

, 2017
Recent advances on antibacterial activity of peptidoglycan recognition proteins (PGRPs) offer some insight into how innate immunity has retained its antimicrobial effectiveness for millions of years with no frequent emergence of resistant strains. First,
Dziarski, Roman, Gupta, Dipika
core   +1 more source

Engineering of a chromogenic enzyme screening system based on an auxiliary indole‐3‐carboxylic acid monooxygenase

MicrobiologyOpen, 2019
Here, we present a proof‐of‐principle for a new high‐throughput functional screening of metagenomic libraries for the selection of enzymes with different activities, predetermined by the substrate being used. By this approach, a total of 21 enzyme‐coding
Vida Časaitė, Mikas Sadauskas, Justas Vaitekūnas, Renata Gasparavičiūtė, Rita Meškienė, Izabelė Skikaitė, Mantas Sakalauskas, Jevgenija Jakubovska, Daiva Tauraitė, Rolandas Meškys   +9 more
doaj   +1 more source

A new crystal form of penicillin acylase from Escherichia coli [PDF]

, 1997
A new crystal form of penicillin acylase (penicillin amidohydrolase, E.C. 3.5.1.11) from Escherichia coli W (ATCC 11105) is reported. The crystals were grown using a combination of hanging-drop and streak-seeding methods.
Brannigan, J.A., Done, S.H., McVey, C.E., Tolley, S.P., Wilson, K.S.   +4 more
core   +2 more sources

Characterization of the metallo-dependent amidohydrolases responsible for “auxiliary” leucinyl removal in the biosynthesis of 2,2′-bipyridine antibiotics

Synthetic and Systems Biotechnology, 2017
2,2′-Bipyridine (2,2′-BiPy) is an attractive core structure present in a number of biologically active natural products, including the structurally related antibiotics caerulomycins (CAEs) and collismycins (COLs).
Ming Chen, Bo Pang, Ya-nan Du, Yi-peng Zhang, Wen Liu   +4 more
doaj   +1 more source

Safety evaluation of the food enzyme urease from the non‐genetically modified Limosilactobacillus reuteri strain 48/72

EFSA Journal, 2022
The food enzyme urease (urea amidohydrolase EC 3.5.1.5) is produced with the non‐genetically modified Limosilactobacillus reuteri strain 48/72 by Nagase (Europa) GmbH.
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, Boet Glandorf, Lieve Herman, Jaime Aguilera, Magdalena Andryszkiewicz, Yi Liu, Giulio diPiazza, Andrew Chesson   +23 more
doaj   +1 more source

Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV

Biomolecules
The ReAV enzyme from Rhizobium etli, a representative of Class 3 L-asparaginases, is sequentially and structurally different from other known L-asparaginases. This distinctiveness makes ReAV a candidate for novel antileukemic therapies.
Kinga Pokrywka, Marta Grzechowiak, Joanna Sliwiak, Paulina Worsztynowicz, Joanna I. Loch, Milosz Ruszkowski, Miroslaw Gilski, Mariusz Jaskolski   +7 more
doaj   +1 more source

SKN-1 regulates stress resistance downstream of amino catabolism pathways

iScience, 2022
Summary: The deleterious potential to generate oxidative stress is a fundamental challenge to metabolism. The oxidative stress response transcription factor, SKN-1/NRF2, can sense and respond to changes in metabolic state, although the mechanism and ...
Phillip A. Frankino, Talha F. Siddiqi, Theodore Bolas, Raz Bar-Ziv, Holly K. Gildea, Hanlin Zhang, Ryo Higuchi-Sanabria, Andrew Dillin   +7 more
doaj   +1 more source

Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV

Frontiers in Chemistry
ReAV, the inducible Class-3 L-asparaginase from the nitrogen-fixing symbiotic bacterium Rhizobium etli, is an interesting candidate for optimizing its enzymatic potential for antileukemic applications.
Kinga Pokrywka, Marta Grzechowiak, Joanna Sliwiak, Paulina Worsztynowicz, Joanna I. Loch, Milosz Ruszkowski, Miroslaw Gilski, Miroslaw Gilski, Mariusz Jaskolski, Mariusz Jaskolski   +9 more
doaj   +1 more source

Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations

Computational and Structural Biotechnology Journal, 2021
Quantum chemical calculations are today an extremely valuable tool for studying enzymatic reaction mechanisms. In this mini-review, we summarize our recent work on several metal-dependent decarboxylases, where we used the so-called cluster approach to ...
Xiang Sheng, Fahmi Himo
doaj   +1 more source

Diverse origins of microbial L-asparaginases and their current miscellaneous applications

Archives of Pharmaceutical Sciences Ain Shams University, 2019
L-asparaginase, also known as amidohydrolase, catalyzes the breakdown of asparagine into aspartic acid and ammonia. Due to its ability to inhibit the biosynthesis of protein lymphoblasts, it is used to treat acute lymphoblastic leukemia (ALL).
Nada A. Abdelrazek, Walid Faisal Elkhatib , Marwa M. Raafat, Mohammad Aboulwafa   +3 more
doaj   +1 more source