Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

New experimental conditions showing the phenomena of "antibiotic tolerance" are described. In Streptococcus pneumoniae, a strong protection against the loss of viability induced by penicillin was obtained when TRIS (hydroxymethyl aminomethane), instead of potassium phosphate, was used as buffer of the growth medium. The main pneumococcal autolysin (N-acetyl-muramil amidase) present in S. pneumoniae was found to be, at least partially, responsible for the loss of viability induced by beta-lactamic molecules.
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PMID:[Influence of the autolytic system on the bactericidal effect induced by beta-lactamic antibiotics (author's transl)]. 740 42

A microbial peptide amidase was found in a limited screening and purified about 500-fold from Stenotrophomonas maltophilia. The native enzyme has a molecular mass of 38 kDa (gel filtration). The sequence of the first 16 amino acids was determined by Edman degradation. The isoelectric point was found to be around 5.8. The peptide amidase exhibited a pH optimum of 6.0 and a temperature optimum of about 39-45 degrees C. The enzyme is stable in 50 mM TRIS/HCl, pH 7.5, at 30 degrees C, and the residual activity was found to be above 90% after 1 week of incubation. The biocatalyst is not inhibited by potential inhibitors like Hg2+, EDTA, D-cycloserine or dithiothreitol and only weakly influenced by inhibitors of serine proteases. The peptide amidase deamidates selectively C-terminal amide groups in peptide amides without hydrolysing internal peptide bonds or amide functions in the side-chain of glutamine or asparagine. Unprotected amino acid amides are not hydrolysed. The enzyme is stereoselective with regard to L-enantiomers in the C-terminal position.
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PMID:Purification and characterization of a newly screened microbial peptide amidase. 859 40