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Literature summary for 4.1.2.25 extracted from

  • Scherperel, G.; Yan, H.; Wang, Y.; Reid, G.E.
    'Top-down' characterization of site-directed mutagenesis products of Staphylococcus aureus dihydroneopterin aldolase by multistage tandem mass spectrometry in a linear quadrupole ion trap (2006), Analyst, 131, 291-302.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E29A multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme yields identical product ion spectrum to the wild-type protein Staphylococcus aureus
E81A multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme yields identical product ion spectrum to the wild-type protein Staphylococcus aureus
K107A multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme is compared to that of wild-type enzyme It yields significantly different product ion spectra dominated by cleaves occuring N-terminal to Pro Staphylococcus aureus
Y61F multistage tandem mass spectrometry (MS/MS and MS3) of gas-phase fragmentation reaction of the mutant enzyme yields identical product ion spectrum to the wild-type protein Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
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