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Results 1 - 5 of 5
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the reaction diagram Show all sequences 1.21.98.4748215 Demonstration that the radical S-adenosylmethionine (SAM) enzyme PqqE catalyzes de novo carbon-carbon cross-linking within a peptide substrate PqqA in the presence of the peptide chaperone PqqD J. Biol. Chem. 291 8877-8884 2016 Methylorubrum extorquens 26961875
Display the reaction diagram Show all sequences 1.21.98.4748215 Demonstration that the radical S-adenosylmethionine (SAM) enzyme PqqE catalyzes de novo carbon-carbon cross-linking within a peptide substrate PqqA in the presence of the peptide chaperone PqqD J. Biol. Chem. 291 8877-8884 2016 Methylorubrum extorquens ATCC 14718 26961875
Display the reaction diagram Show all sequences 1.21.98.4747504 Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily Chem. Commun. (Camb.) 46 7031-7033 2010 Klebsiella pneumoniae 20737074
Display the reaction diagram Show all sequences 1.21.98.4748189 PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway J. Biol. Chem. 290 12908-12918 2015 Methylorubrum extorquens 25817994
Display the reaction diagram Show all sequences 1.21.98.4748189 PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway J. Biol. Chem. 290 12908-12918 2015 Methylorubrum extorquens ATCC 14718 25817994
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