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Literature summary for 1.1.5.2 extracted from

  • Puehringer, S.; RoseFigura, J.; Metlitzky, M.; Toyama, H.; Klinman, J.P.; Schwarzenbacher, R.
    Structural studies of mutant forms of the PQQ-forming enzyme PqqC in the presence of product and substrate (2010), Proteins, 78, 2554-2562.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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Klebsiella pneumoniae MGH 78578
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Synonyms

Synonyms Comment Organism
PqqC
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Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone i.e. 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid, prosthetic group, not covalently linked to the polypeptide chain or posttranslationally derived from precursor amino acid residues in the active site of the constituent. enzyme. Biosynthesis of the cofactor in Klebsiella pneumoniae is facilitated by six genes, pqqABCDEF. PqqC is one of two metal free oxidases of known structure and catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid, overview Klebsiella pneumoniae