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Results 1 - 10 of 110 > >>
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13dansyl-UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate - Escherichia coli UMP + dansyl-UDP-NAc-muramoyl-pentapeptide-diphosphoundecaprenol - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate Staphylococcus aureus ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate Escherichia coli ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more all five cytoplasmic segments contribute to catalytic site with at least 14 invariant polar and/or charged, non-clustered residues, conserved residue D98 supposedly involved in deprotonation of lipid substrate during catalysis at physiological pH 7.4 (pKa for undecaprenyl phosphate: 6.6 and 9.2) Bacillus subtilis ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more functional complementation in a MraY-lacking, thermosensitive Escherichia coli mutant strain (2fold increased UDP-N-acetylmuramoyl-pentapeptide level compared to wild-type cells when grown 30 min at 42°C, depletion of lipid I) by overexpression of wild-type or mutants E299Q, D177N, N168A, H45R, K48Q, H291R Bacillus subtilis ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more UDP-N-acetylmuramyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine: Parkย’s nucleotide, UDP-MurNAc-pentapeptide Bacteria ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more assay method development for high-throughput screening assays and metadata annotation, overview Bacillus subtilis ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate Bacillus subtilis ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more assay method development for high-throughput screening assays and metadata annotation, overview Bacillus subtilis 168 ? - ?
Show all pathways known for 2.7.8.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.8.13more the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate Bacillus subtilis 168 ? - ?
Results 1 - 10 of 110 > >>