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Ligand pyrroloquinoline quinone
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Basic Ligand Information
2,7,9-tricarboxypyrroloquinoline quinone, 4,5-Dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid, 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, PQQ, pyrroliquinoline quinone, pyrrolo-quinoline quinone, pyrroloquinoline-quinone, pyrrolquinoline quinone, vitamin PQQ
Show all BRENDA pathways known for pyrroloquinoline quinone
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)
top
EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
D-glucose + pyrroloquinoline quinone = D-glucono-1,5-lactone + pyrroloquinoline quinol
quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone
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(S)-2-hydroxyglutarate + pyrroloquinoline quinone = 2-oxoglutarate + pyrroloquinoline quinol
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In Vivo Product in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
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
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
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
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
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
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
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
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
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
Substrate in Enzyme-catalyzed Reactions (60 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
diethylstilbestrol + pyrroloquinoline quinone = diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
2-amino-D-glucose + pyrroloquinoline quinone = 2-amino-D-glucono-1,5-lactone + pyrroloquinoline quinol
2-deoxy-D-glucose + pyrroloquinoline quinone = 2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
3-deoxy-D-glucose + pyrroloquinoline quinone = 3-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
3-O-methyl-D-glucose + pyrroloquinoline quinone = 3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
6-deoxy-D-glucose + pyrroloquinoline quinone = 6-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
D-allose + pyrroloquinoline quinone = D-allono-1,5-lactone + pyrroloquinoline quinol
D-galactose + pyrroloquinoline quinone = D-galactono-1,5-lactone + pyrroloquinoline quinol
D-glucose + pyrroloquinoline quinone = D-glucono-1,5-lactone + pyrroloquinoline quinol
D-mannose + pyrroloquinoline quinone = D-mannono-1,5-lactone + pyrroloquinoline quinol
D-ribose + pyrroloquinoline quinone = D-ribono-1,5-lactone + pyrroloquinoline quinol
D-xylose + pyrroloquinoline quinone = D-xylono-1,5-lactone + pyrroloquinoline quinol
L-arabinose + pyrroloquinoline quinone = L-arabino-1,5-lactone + pyrroloquinoline quinol
L-rhamnose + pyrroloquinoline quinone = L-rhamnono-1,5-lactone + pyrroloquinoline quinol
D-fucose + pyrrolquinoline quinone = 6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
2-butanol + pyrroloquinoline quinone = butane-2-one + reduced pyrroloquinoline quinone
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cyclopentanol + pyrroloquinoline quinone = cyclopentanone + pyrroloquinoline quinol
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quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone
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(S)-2-hydroxyglutarate + pyrroloquinoline quinone = 2-oxoglutarate + pyrroloquinoline quinol
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lupanine + pyrroloquinoline quinone + H2O = 17-hydroxylupanine + pyrroloquinoline quinol
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Product in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
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
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
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
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
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
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
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
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
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
Enzyme Cofactor/Cosubstrate (383 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+
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PQQ, PQQ is synthesized in the cytosol, but the proteins that use it are periplasmic, it might bind to subunit XoxJ near or at residue W200, no binding to XoxJ mutant W200F. Metal-bound PQQ is bound at subunit XoxF
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enzyme expressed in Escherichia coli requires pyrroloquinoline quinone for activity
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functions as a coenzyme, mutant strain NDl (a polyvinyl alcohol oxidase-deficient mutant of Pseudomonas sp. strain VM15C) grows on polyvinyl alcohol and required PQQ for utilization of polyvinyl alcohol as an essential growth factor
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the enzyme purified in presence of EDTA shows no activity until pyrroloquinoline quinone, Ca2+, Mg2+ are added
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PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GAGNPG in PedE, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster
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PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GLGVQG and GSGVLG in PedH, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster
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pyrroloquinoline quinone-dependent enzyme. The enzyme binds to pyrroloquinoline quinone at a ratio of 1: 1
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one pyrroquinoline covalently bound to one molecule, additional two-electron redox center
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quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
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apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
contains one pyrroloquinoline quinone per subunit, pyrroloquinoline quinone (PQQ) is 2,7,9 tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione
during the processing of pyrroloquinoline quinone into the apoenzyme to give active enzyme, its affinity is markedly dependent on the pH, four groups with pK values between pH 7 and pH 8 are involved
each subunit of the dimer contains one molecule of 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
i.e. PQQ, dependent on exogenous PQQ, since Escherichia coli does not synthesize PQQ itself
i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity
i.e. PQQ, dependent on, functions as a redox mediator by transfer of hydride ions and electrons, redox-related structural changes, overview
i.e. PQQ, or 2,7,9-tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione, residues Gln231, Gln246, Ala350, and Leu376 are involved in binding
PQQ, essential cofactor for enzyme activity, essential role of pqqABCDEF in PQQ biosynthesis, overview
prosthetic group
reconstitution of the apoenzyme to full activity is achieved with a stoichiometric amount of pyrroloquinoline quinone. Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
Sinorhizobium meliloti is unable to synthesize pyrroloquinoline quinone, synthesis of the holoenzyme in alfalfa nodules
the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+
type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid
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one pyrroloquinoline quinone is associated with one molecule of the purified ADH complex
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PQQ, active in electron transfer, a tightly bound ubiquinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase. The enzyme possesses distinct quinone oxidation, reduction and high affinity binding sites, analysis, overview
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PQQ, subunit I contains pyrroloquinoline quinone and heme c, and subunit II contains three heme c components
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PQQ, the PQQ ring is sandwiched between the indole ring of Trp245 and the two sulfur atoms of the disulfide ring structure
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PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
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pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone is coordinated by Q87, I135, R137, S181, R350, L413, N417, W418, and W493. The side chains of W263 and the vicinal disulfide bond between C131 and C132 provide additional stacking interactions
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only pyrroloquinoline quinone is effective as electron acceptor, no activity with FAD, FMN and NAD(P)+
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binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer
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holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity
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the cofactor transfers redox equivalents to the respiratory chain during the biotransformation of NHEG to 6NSL
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reconstitution mechanism of the enzyme (sGDH) with its two cofactors, i.e., pyrroloquinoline quinone (PQQ) and Ca2+: pyrroloquinoline quinone first binds to apo-sGDH, it strongly impedes the access of Ca2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. The slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca2+ binding loop through the specific mutation of the calcium-coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion
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soluble isoform sGDH is able to bind two mol of PQQ in one mol of the homodimer with high affinity. The binding reaction is much faster at alkaline pH than at acidic pH and requires the presence of some divalent cations such as Cd2+, Ca2+, Sr2+, or Mn2+. Membrane-bound isoform mGDH binds one mol of PQQ in the monomeric enzyme with a relatively slow reaction process, which has an optimim at acidic pH and in the presence of divalent cations such as Mg2+, Ca2+, Zn2+, Sr2+. Binding of PQQ affects the conformation of both isoforms
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the catalytic potential of the cofactor in the enzyme is not determined by its adduct-forming ability but by whether it is or can be activated with Ca2+
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quinohaemoprotein, contains a molecule of pyrroloquinoline quinone. The heme accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone)
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pyrroloquinoline quinone-to-subunit stochiometry of approximately 1:1, 3.6 mol of pyrroloquinoline quinone per mol of enzyme
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after reconstitution to the holoenzyme by the addition of pyrroloquinoline quinone, addition of substrate changes the absorption spectrum to that of reduced cytochrome c, indicating that the heme c group participates in the enzymic mechanism, one molecule of pyrroloquinoline quinone is bound per enzyme molecule
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electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c to the membrane ubiquinone
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PQQ, a prosthetic group, ADH I is a non-heme quinoprotein containing 2.2 mol of PQQ per mol of enzyme
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PQQ, a prosthetic group, isozyme ADH IIB is a quinohemoprotein dehydrogenase. ADH IIB contains 1.4 mol of PQQ per mol of enzyme on the basis of a molecular weight of 70000 Da
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PQQ, a prosthetic group, isozyme ADH IIG is a quinohemoprotein dehydrogenase. ADH IIG contains 1.2 mol of PQQ per mol of enzyme on the basis of a molecular weight of 70000 Da
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prosthetic group, covalently bound pyrroloquinoline quinone, PQQ or a compound which closely resembles PQQ
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Activator in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
absolutely required for activity, one mole of PQQ is bound to one mole of apoenzyme
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essential for polyvinyl alcohol degradation, another yet unknown growth factor supplied by co-isolated Rhodococcus erythropolis strain
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Inhibitor in Enzyme-catalyzed Reactions (4 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
3D Structure of Enzyme-Ligand-Complex (PDB) (313 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
KM Value (22 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0035
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pH 5.0, 25°C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside
0.0035
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ubiquinone-bound enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C
0.0064
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pH 5.0, 25°C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside
0.0064
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Ubiquinone-free enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C
References & Links
Literature References (233)
Links to other databases for pyrroloquinoline quinone
ChEBI
PubChem
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Release 2023.1 (January 2023)
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