Information on EC 1.3.3.11 - pyrroloquinoline-quinone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.3.11
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RECOMMENDED NAME
GeneOntology No.
pyrroloquinoline-quinone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyrroloquinoline quinone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing)
So far only a single turnover of the enzyme has been observed, and the pyrroloquinoline quinone remains bound to it. It is not yet known what releases the product in the bacterium.
CAS REGISTRY NUMBER
COMMENTARY hide
353484-42-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KR1, extremely radioresitant
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Manually annotated by BRENDA team
strain KR1, extremely radioresitant
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Manually annotated by BRENDA team
subsp. pneumoniae
UniProt
Manually annotated by BRENDA team
strain AM1rif, enzyme appears to be a fusion protein of PqqC and PqqD
Swissprot
Manually annotated by BRENDA team
gene pqqC
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the gene pqqC is a suitable molecular marker that can be used complementary to housekeeping genes for studying the diversity and evolution of plant-beneficial pseudomonads, phylogenetic tree, overview. Phylogenetic distribution of cultivated and noncultivated pseudomonads from wheat roots based on pqqC
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid + O2
4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
show the reaction diagram
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8,-octahydroquinoline-2,4-dicarboxylate + O2
4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
show the reaction diagram
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2
4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid + O2
4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
show the reaction diagram
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8,-octahydroquinoline-2,4-dicarboxylate + O2
4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + H2O2 + H2O
show the reaction diagram
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2
4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PqqC is a metal free oxidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxidized pyrroloquinoline quinone
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pyrroloquinoline quinone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
activating factor ActF
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dithioerythritol
dithiothreitol
NAD(P)H
TrxAB
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the complete TrxAB system enhance the pyrroloquinoline quinone production
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additional information
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no dependence on NADH or NADPH in purified enzyme preparation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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calculated from deduced amino acid sequence
5.73
calculated from the deduced amino acid sequence
PDB
SCOP
CATH
ORGANISM
UNIPROT
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
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SDS-PAGE
113000
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gel filtration
150000
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determined by gel filtration, with DTT
300000
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determined by gel filtration, without DTT
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
trimer
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3 * 42000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutants H154S/PQQ Y175F/PQQ Y175S/R179S in complex with intermediate 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid, sitting drop-vapor diffusion method, optimized conditions for each mutant: 0.1 M HEPES, pH 7.0, 0.5% w/v PEG 8000 for mutant H154S/PQQ complex, 0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% w/v PEGl 3350 for mutant Y175F/PQQ complex, and 0.2 M sodium chloride, 0.1 M Tris, pH 8.5, 25% w/v PEG 3350 for mutant R179S/Y175S/intermediate complex, all at 20C, X-ray diffraction structure determination and analysis at 1.3-2.35 A resolution
sitting drop vapor diffusion method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Superdex S-200 gel filtration
partial purification of recombinant protein
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Q-Sepharose column chromatography and Ultrogel AcA54 gel filtration
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recombinant His-tagged wild-type and mutant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)pLysS, complements the mineral phosphate solubilization phenotype
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expressed in Escherichia coli DH alpha, complementation studies with PqqC deficient Methylobacterium extorquens and Methylobacterium organophilum
expressed in Escherichia coli DHalpha
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gene pqqC, expression of wild-type and mutant enzymes as His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene pqqC, from a Pseudomonas strain collection and from a natural wheat rhizosphere population, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H154S
site-directed mutagenesis, active site mutant, even with substrate PQQ bound, the enzyme is still in the open conformation with helices alpha5b and alpha6 unfolded and the active site solvent accessible, no product formation
H84A
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active site mutant with reduced activity
H84N
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active site mutant with reduced activity
R179S/Y175S
site-directed mutagenesis, active site mutant, the mutant shows an open conformation with a reaction intermediate trapped in the active site, the intermediate is tricyclic but nonplanar, implying that it has not undergone oxidatio, R179S/Y175S shows acceptable substrate complex crystals
Y175F
site-directed mutagenesis, active site mutant, the mutant shows a closed conformation indicating that Y175 is not required for the conformational change, no product formation
H154S
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site-directed mutagenesis, active site mutant, even with substrate PQQ bound, the enzyme is still in the open conformation with helices alpha5b and alpha6 unfolded and the active site solvent accessible, no product formation
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R179S/Y175S
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site-directed mutagenesis, active site mutant, the mutant shows an open conformation with a reaction intermediate trapped in the active site, the intermediate is tricyclic but nonplanar, implying that it has not undergone oxidatio, R179S/Y175S shows acceptable substrate complex crystals
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Y175F
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site-directed mutagenesis, active site mutant, the mutant shows a closed conformation indicating that Y175 is not required for the conformational change, no product formation
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additional information
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N60I mutation detected in PqqC deficiency mutant
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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the gene pqqC is a suitable molecular marker that can be used complementary to housekeeping genes for studying the diversity and evolution of plant-beneficial pseudomonads
Show AA Sequence (1541 entries)
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