Results 1 to 10 of about 4,894 (170)
Comparative Analysis of Mesophilic YqfB-Type Amidohydrolases
Biomolecules, 2022 The widespread superfamily of the human activating signal cointegrator homology (ASCH) domain was identified almost 20 years ago; however, the amount of experimental data regarding the biological function of the domain is scarce.
Roberta Statkevičiūtė +4 more
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Crystal structure of N-carbamyl-d-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases [PDF]
Structure, 2000 N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we
Eiki Yamashita +2 more
exaly +3 more sources
Biomolecules, 2023 The activity of β-ureidopropionase, which catalyses the last step in the degradation of uracil, thymine, and analogous antimetabolites, is cooperatively regulated by the substrate and product of the reaction.
Daniela Cederfelt +5 more
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Identification of a metabolic-related gene signature predicting the overall survival for patients with stomach adenocarcinoma [PDF]
PeerJ, 2021 Background The reprogramming of energy metabolism and consistently altered metabolic genes are new features of cancer, and their prognostic roles remain to be further studied in stomach adenocarcinoma (STAD).
Yuan Nie, Linxiang Liu, Qi Liu, Xuan Zhu
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Structure of the Ergothioneine‐Biosynthesis Amidohydrolase EgtC [PDF]
ChemBioChem, 2015 AbstractThe ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nα‐trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use γ‐glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of γ‐glutamyl cysteine is removed by the glutamine
Vit, Allegra +3 more
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Penicillin Amidohydrolases in Fungal Autolysis [PDF]
Microbiology and Immunology, 1989 AbstractThe production of penicillin G and penicillin V amidohydrolases or acylases (E.C.3.5.1.11) was studied during the autolysis of filamentous fungi in a mineral medium, and in the same medium with phenoxyacetic acid as inducer. In all the studied fungi, enzymes showing penicillin G and penicillin V amidohydrolase activities were found.
C, Alfonso, L, Cribeiro, F, Reyes
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Biochemical and Genetic Analysis of 4-Hydroxypyridine Catabolism in Arthrobacter sp. Strain IN13
Microorganisms, 2020 N-Heterocyclic compounds are widely spread in the biosphere, being constituents of alkaloids, cofactors, allelochemicals, and artificial substances. However, the fate of such compounds including a catabolism of hydroxylated pyridines is not yet fully ...
Justas Vaitekūnas +4 more
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Microbiology Spectrum, 2022 Ochratoxin A (OTA) is a potent mycotoxin mainly produced by toxicogenic strains of Aspergillus spp. and seriously contaminates foods and feedstuffs. OTA detoxification strategies are significant to food safety.
Nan Chen +6 more
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Phenoxymethylpenicillin amidohydrolases from Penicillium chrysogenum [PDF]
FEBS Letters, 1996 A phenoxymethylpenicillin amidohydrolase which hydrolyses phenoxymethylpenicillin to 6‐aminopenicillanic acid (6‐APA) has been isolated from two species of Penicillium chrysogenum. The amidohydrolase had a molecular mass of approx. 42 kDa. Its activity with benzylpenicillin as substrate was only 1.5% of that with phenoxymethylpenicillin and it was ...
Whiteman, P.A., Abraham, E.P.
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Stem Cell Research, 2021 Farber disease is an ultra-rare lysosomal storage disease. Mutations in the N-acylsphingosine amidohydrolase (ASAH1) gene, which encodes for the enzyme acid ceramidase (ACDase), cause ceramides to accumulate in the body.
Brianna M. Brooks +8 more
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