Results 11 to 20 of about 6,806 (259)
Auxin Amidohydrolases – From Structure to Function: Revisited [PDF]
Croatica Chemica Acta, 2018 The control of plant growth and development is a well-coordinated process between exogenous and endogenous signals. Auxins are plant hormones belonging to the endogenous signals, which control a vast array of different processes.
Ana Smolko +2 more
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On the Origin of Substrate Specificity of Enzymes from the Amidohydrolase Superfamily. [PDF]
Angew Chem Int Ed EnglComprehensive analyses of two enzyme classes from the amidohydrolase superfamily (AHS) revealed that catalysis proceeds either via 1,4 or 1,6 nucleophilic conjugate addition and that this property defines substrate specificity. Moreover, although all substrates and products are entirely achiral, this mechanistic difference results in an inverted ...
Drexler L +3 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 ...
Pat Whiteman, E. P. Abraham
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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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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
A. Vit +3 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
T. Nakai +11 more
semanticscholar +3 more sources
Molecules, 2021 Dihydroorotase (DHOase), a dimetalloenzyme containing a carbamylated lysine within the active site, is a member of the cyclic amidohydrolase family, which also includes allantoinase (ALLase), dihydropyrimidinase (DHPase), hydantoinase, and imidase ...
Hong-Hsiang Guan +4 more
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Eclética Química, 2021 Ureases are amidohydrolases that catalyze the hydrolysis of urea to ammonia and carbamate. In addition to the enzymatic function, ureases have fungitoxic and insecticidal function, which are independent of their catalytic activity.
Elisângela Andrade Ângelo +8 more
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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 ...
Lan Hu +2 more
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Purification and Characterization of an ATP‐dependent Amidohydrolase, N‐methylhydantoin Amidohydrolase, from Pseudomonas putida 77 [PDF]
European Journal of Biochemistry, 1995 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.
J, Ogawa +5 more
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