Results 51 to 60 of about 3,796 (188)

Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

, 2016
Background: Pseudomonas aeruginosa, a Gram-negative, aerobic coccobacillus bacterium is an opportunistic human pathogen and worldwide the fourth most common cause of hospital-acquired infections which are often high mortality such as ventilator ...
Krämer, Andreas, Overhage, Jörg, Meyer-Almes, Franz-Josef, Franz-Josef Meyer-Almes, Joerg Overhage, Jan Herzer, Andreas Krämer, Herzer, Jan   +7 more
core   +1 more source

The Hemoprotein Hhy1 Promotes Heme‐Dependent Catalase Activity of Ctt1

Molecular Microbiology, Volume 125, Issue 5, Page 389-411, May 2026.
A Schizosaccharomyces pombe strain deficient in heme (hem1Δ) and siderophore (Fc) biosynthesis, as well as high‐affinity iron (Fe) uptake (blue), was used to uncover the hemoprotein Hhy1 that promotes the heme‐dependent activity of the catalase Ctt1. In contrast, hhy1Δ cells exhibit reduced Ctt1 activity and increased sensitivity to oxidative stress ...
Tobias Vahsen, Samuel Plante, Berthy Mbuya, Simon Labbé   +3 more
wiley   +1 more source

Determination of cephalosporin-C amidohydrolase activity with fluorescamine

Journal of Pharmacy and Pharmacology, 1989
Abstract A spectrophotometric procedure for the assay of cephalosporin-C amidohydrolase activity, based on the determination of the 7-aminocephalosporanic acid (7-ACA) produced in the hydrolysis of cephalosporin-C by the enzyme, is described. This procedure can be used to detect 7-ACA over a range of 10 to 200 μg mL−1.
F, Reyes, M J, Martinez, J, Soliveri
openaire   +2 more sources

The Hydrolysis of Amides and the Proficiency of Amidohydrolases. The Burden Borne by k_w

, 2016
The hydrolysis of small amides has garnered major attention due to its relevance to peptide hydrolysis, one of the most fundamental reactions of biology. Both experimental and theoretical research efforts have studied the reaction in different media, and
Guillermina Estiu (105847), Kenneth M. Merz (1311057)   +1 more
core   +1 more source

Safety evaluation of the food enzyme glutaminase from the genetically modified Bacillus subtilis strain Glu3‐3

EFSA Journal, Volume 24, Issue 5, May 2026.
Abstract The food enzyme glutaminase (l‐glutamine amidohydrolase; EC 3.5.1.2) is produced with the genetically modified Bacillus subtilis strain Glu3‐3 by Angel Yeast Co., Ltd. The production strain of the food enzyme contains multiple copies of acquired antimicrobial resistance genes.
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, Henk Van Loveren, Laurence Vernis, Jaime Aguilera, Magdalena Andryszkiewicz, Daniele Cavanna, Yi Liu   +16 more
wiley   +1 more source

Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida [PDF]

Journal of Bacteriology, 1987
Formylglutamate amidohydrolase (FGase) catalyzes the terminal reaction in the five-step pathway for histidine utilization in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolyzed to produce L-glutamate plus formate. Urocanate, the first product in the pathway, induced all five enzymes, but FG was able to induce FGase alone ...
L, Hu, L M, Mulfinger, A T, Phillips
openaire   +2 more sources

Identification, biochemical characterization, and subcellular localization of allantoate amidohydrolases from Arabidopsis and soybean

, 2008
Allantoate amidohydrolases (AAHs) hydrolize the ureide allantoate to ureidoglycolate, CO(2), and two molecules of ammonium. Allantoate degradation is required to recycle purine-ring nitrogen in all plants.
Witte, Claus-Peter, Sparkes, Imogen A, Romeis, Tina, Werner, Andrea K   +3 more
core   +1 more source

Safety evaluation of the food enzyme amidase from the genetically modified Escherichia coli strain SP‐a

EFSA Journal, Volume 24, Issue 5, May 2026.
Abstract The food enzyme amidase (acylamide amidohydrolase, EC 3.5.1.4) is produced with the genetically modified Escherichia coli strain SP‐a by c‐LEcta GmbH. The genetic modifications did not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
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, Henk Van Loveren, Laurence Vernis, Cristina Fernàndez‐Fraguas, Daniele Cavanna, Ana Criado, Simone Lunardi, Yi Liu   +17 more
wiley   +1 more source

Biochemical properties of penicillin amidohydrolase from Micrococcus luteus [PDF]

Applied and Environmental Microbiology, 1979
Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C.
D H, Nam, D D, Ryu
openaire   +2 more sources

Biopharmaceuticals for Cancer Treatment: An Update

Cancer Medicine, Volume 15, Issue 4, April 2026.
ABSTRACT Cancer is one of the most debilitating diseases, causing profound physical and psychological impacts on patients. The global number of cancer patients has been steadily rising over the last few decades. The development of effective cancer therapies remains the primary focus in life science research, requiring a precise understanding of ...
Anupom Deb Nath, Yousuf Alam, Afsana Mustak Mim, Maksuda Akter, Mohammad Abbas Gani, Khondaker Muhammad Khairul Alam, Md. Nur Alam   +6 more
wiley   +1 more source