Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Puehringer, S.; Metlitzky, M.; Schwarzenbacher, R.
    The pyrroloquinoline quinone biosynthesis pathway revisited: a structural approach (2008), BMC Biochem., 9, 8-8.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.11 29000
-
 2 * 29000, PqqC, SDS-PAGE Escherichia coli
1.3.3.11 29000
-
 2 * 29000, PqqC, SDS-PAGE Pseudomonas aeruginosa
1.3.3.11 29000
-
 2 * 29000, PqqC, SDS-PAGE Klebsiella pneumoniae
1.3.3.11 58000
-
 PqqC, SDS-PAGE Escherichia coli
1.3.3.11 58000
-
 PqqC, SDS-PAGE Pseudomonas aeruginosa
1.3.3.11 58000
-
 PqqC, SDS-PAGE Klebsiella pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.11 Escherichia coli
-
-
-
1.3.3.11 Klebsiella pneumoniae P27505
-
-
1.3.3.11 Pseudomonas aeruginosa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.3.11 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O PqqC is part of a complex of six enzymes that act together in pyrroloquinoline-quinone synthesis: PqqA serves as a complex precursor for for pyrroloquinoline-quinone synthesis, PqqB is not directly required for pyrroloquinoline-quinone biosynthesis, but a carrier and responsible for its transport across the plasma-membrane into the periplasm, PqqC does not contain a redox-active metal or other cofactor and is responsible for the last cyclization and oxidation steps in pyrroloquinoline-quinone synthesis, PqqD has three possible functions: first, it could play a role in the release of pyrroloquinoline-quinone from PqqC, second it could be involved in binding of PqqB to PqqC, third it could function as the dioxygenase in the pathway, PqqE is a family member of radical S-adenosylmethionine enzymes and catalyzes a radical driven C-C bond formation required to link the glutamate and tyrosine moieties at atoms C9 and C9a of pyrroloquinoline-quinone, PqqF recognizes and cleaves all four peptide bonds in PqqA Klebsiella pneumoniae
a
1.3.3.11 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O PqqC is part of a complex of six enzymes that act together in pyrroloquinoline-quinone synthesis: PqqA serves as a complex precursor for for pyrroloquinoline-quinone synthesis, PqqB is not directly required for pyrroloquinoline-quinone biosynthesis, but a carrier and responsible for its transport across the plasma-membrane into the periplasm, PqqC does not contain a redox-active metal or other cofactor and is responsible for the the last cyclization and oxidation steps in pyrroloquinoline-quinone synthesis, PqqD has three possible functions: first, it could play a role in the release of pyrroloquinoline-quinone from PqqC, second it could be involved in binding of PqqB to PqqC, third it could function as the dioxygenase in the pathway, PqqE is a family member of radical S-adenosylmethionine enzymes and catalyzes a radical driven C-C bond formation required to link the glutamate and tyrosine moieties at atoms C9 and C9a of pyrroloquinoline-quinone, PqqF recognizes and cleaves all four peptide bonds in PqqA Pseudomonas aeruginosa
a
1.3.3.11 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O PqqC is part of a complex of six enzymes that act together in pyrroloquinoline-quinone synthesis: PqqA serves as a complex precursor for for pyrroloquinoline-quinone synthesis, PqqB is not directly required for pyrroloquinoline-quinone biosynthesis, but a carrier and responsible for its transport across the plasma-membrane into the periplasm, PqqC does not contain a redox-active metal or other cofactorand is responsible for the the last cyclization and oxidation steps in pyrroloquinoline-quinone synthesis, PqqD has three possible functions: first, it could play a role in the release of pyrroloquinoline-quinone from PqqC, second it could be involved in binding of PqqB to PqqC, third it could function as the dioxygenase in the pathway, PqqE is a family member of radical S-adenosylmethionine enzymes and catalyzes a radical driven C-C bond formation required to link the glutamate and tyrosine moieties at atoms C9 and C9a of pyrroloquinoline-quinone, PqqF recognizes and cleaves all four peptide bonds in PqqA Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.11 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid + O2
-
 Escherichia coli 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
-
 ?
1.3.3.11 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid + O2
-
 Pseudomonas aeruginosa 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
-
 ?
1.3.3.11 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid + O2
-
 Klebsiella pneumoniae 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.3.11 homodimer 2 * 29000, PqqC, SDS-PAGE Escherichia coli
1.3.3.11 homodimer 2 * 29000, PqqC, SDS-PAGE Pseudomonas aeruginosa
1.3.3.11 homodimer 2 * 29000, PqqC, SDS-PAGE Klebsiella pneumoniae

Synonyms

EC Number Synonyms Comment Organism
1.3.3.11 PqqC
-
 Escherichia coli
1.3.3.11 PqqC
-
 Pseudomonas aeruginosa
1.3.3.11 PqqC
-
 Klebsiella pneumoniae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.3.3.11 Escherichia coli PqqC, theoretical value
-
 5.9
1.3.3.11 Pseudomonas aeruginosa PqqC, theoretical value
-
 5.9
1.3.3.11 Klebsiella pneumoniae PqqC, theoretical value
-
 5.9