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  • 14 Hits
  • Search Condition : Filter (MeSH = Amidohydrolases / metabolism*)
Species Resource
Pathogenic microorganisms IFM 46114 , IFM 40505 Screening of chitin deacetylase from Mucoralean strains (Zygomycetes) and its relationship to cell growth rate.
Rats Identification and distribution of aspartoacylase in the postnatal rat brain.
Rats TRM/Kyo(strainID=11) Restoration of aspartoacylase activity in CNS neurons does not ameliorate motor deficits and demyelination in a model of Canavan disease.
Rats TRM/Kyo(strainID=11) Effects of AAV-2-mediated aspartoacylase gene transfer in the tremor rat model of Canavan disease.
General Microbes JCM 3132 Defining sequence space and reaction products within the cyanuric acid hydrolase (AtzD)/barbiturase protein family.
Pathogenic microorganisms JCM 12137? , JCM 11569? , JCM 11571? , JCM 12611? Microbacterium natoriense sp. nov., a novel D-aminoacylase-producing bacterium isolated from soil in Natori, Japan.
Cellular slime molds G02262 Eukaryotic beta-alanine synthases are functionally related but have a high degree of structural diversity.
Prokaryotes E. coli ? Inefficient Tat-dependent export of periplasmic amidases in an Escherichia coli strain with mutations in two DedA family genes.
Prokaryotes E. coli ME9062(BW25113) , JW5646-KC , JW2712-KC , JW1667-KC Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis.
Prokaryotes E. coli NA Identification of nitrile hydratase-producing Rhodococcus ruber TH and characterization of an amiE-negative mutant.
Drosophila Negative regulation by amidase PGRPs shapes the Drosophila antibacterial response and protects the fly from innocuous infection.
General Microbes Bacillus D-stereospecific metallo-amidohydrolase: active-site metal-ion substitution changes substrate specificity.
General Microbes JCM 10489 Application of protein N-terminal amidase in enzymatic synthesis of dipeptides containing acidic amino acids specifically at the N-terminus.
General Microbes JCM 12893 Enhancing the promiscuous phosphotriesterase activity of a thermostable lactonase (GkaP) for the efficient degradation of organophosphate pesticides.