Comparative Genomic and Transcriptomic Analysis Reveals Why Paenarthrobacter Strains Are Specialists in the Degradation of the Fungicide Iprodione. [PDF]
Microb BiotechnolPaenarthrobacter are specialists in degrading the fungicide iprodione. We showed that this trait has evolved through gene duplication of ipaH and ddaH genes, being in the core genome of paenarthrobacters, and further genetic optimisation, with different strains being at different evolution stages depending on their prior exposure to iprodione ...
Michelioudakis V +7 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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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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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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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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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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Isolation of differentially expressed genes involved in clubroot disease
Plant Protection Science, 2002 The interaction between Plasmodiophora brassicae and its host Brassica rapa is investigated by two strategies. (1) IAA-conjugate hydrolases: Root hypertrophy in club root disease is dependent on increased auxin levels and these could result from auxin ...
A. Schuller, J. Ludwig-Müller
doaj +1 more source
Biochemical characterization of a new nicotinamidase from an unclassified bacterium thriving in a geothermal water stream microbial mat community. [PDF]
PLoS ONE, 2017 Nicotinamidases are amidohydrolases that convert nicotinamide into nicotinic acid, contributing to NAD+ homeostasis in most organisms. In order to increase the number of nicotinamidases described to date, this manuscript characterizes a nicotinamidase ...
Rubén Zapata-Pérez +5 more
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Features of phospho- and amidohydrolases functioning in edaphotopes polluted by ore mill effluents
Vìsnik Dnìpropetrovsʹkogo Unìversitetu: Serìâ Bìologìâ, Ekologìâ, 2006 Influence of aerotechnogenic contamination of soils on activity of some hydrolytic enzymes of nitrogen and phosphorus cycles is examined. Biochemical mobilization of organophosphorous and nitrogen-bearing compounds in soils polluted by heavy metals is ...
O. M. Artyushenko, V. O. Negulyaev
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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
Nakai, T. +10 more
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