Results 21 to 30 of about 10,587 (231)
Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida [PDF]
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 ...
Lan Hu +2 more
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Penicillin Amidohydrolases in Fungal Autolysis [PDF]
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.
Lourdes Cribeiro +2 more
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Thiazoline-Specific Amidohydrolase PurAH Is the Gatekeeper of Bottromycin Biosynthesis [PDF]
The ribosomally synthesized and post-translationally modified peptide (RiPP) bottromycin A2 possesses potent antimicrobial activity. Its biosynthesis involves the enzymatic formation of a macroamidine, a process previously suggested to require the concerted efforts of a YcaO enzyme (PurCD) and an amidohydrolase (PurAH) in vivo. In vitro, PurCD alone is
Asfandyar Sikandar +4 more
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Structure of the Ergothioneine‐Biosynthesis Amidohydrolase EgtC [PDF]
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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Phenoxymethylpenicillin amidohydrolases from Penicillium chrysogenum [PDF]
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 ...
Edward P. Abraham, P.A. Whiteman
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Biochemical and Genetic Analysis of 4-Hydroxypyridine Catabolism in Arthrobacter sp. Strain IN13
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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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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Purification and Characterization of an ATP‐dependent Amidohydrolase, N‐methylhydantoin Amidohydrolase, from Pseudomonas putida 77 [PDF]
N‐Methylhydantoin amidohydrolase, an ATP‐dependent amidohydrolase involved in microbial degradation of creatinine, was purified 70‐fold to homogeneity, with a 62% overall recovery, and was crystallized from Pseudomonas putida 77. The enzyme has a relative molecular mass of 300000.
Jun Ogawa +5 more
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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
doaj +1 more source
Ochratoxin A (OTA) is a well-known, natural contaminant in foods and feeds because of its toxic effects, such as nephrotoxicity in various animals. Recent studies have revealed that Alcaligenes faecalis could generate enzymes to efficiently degrade OTA ...
Honghai Zhang +4 more
doaj +1 more source

