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Results 1 - 10 of 10
EC Number
General Information
phylogenetic analysis of the pqqC gene of species of the genus Pseudomonas reveals that strain JX22 differs significantly from other species with sequenced pqqC genes
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
pqqC gene disruption mutant JX22MT1 by the EZ-Tn5 transposon mutation, the mutant shows no antifungal activity against Fusarium oxysporum f. sp. lycopersici in contrast to the wild-type strain JX22. Antifungal activity at wild-type level is restored by introduction of the functional wild-type pqqC gene
PqqC catalyzes the last step of pyrroloquinoline quinone 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
the enzyme catalyzes the final step of the pyrroloquinoline quinone biosynthesis, namely, cyclization and oxidation of the intermediate 3a-(2-amino-2-carboxy-ethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid to pyrroloquinoline quinone
an all atom model of the quinoprotein dehydrogenase PqqC in complex with 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid (PQQ) and O2, solvated with TIP3 water in periodic boxes, is subjected to random-acceleration molecular dynamics (RAMD) showing that O2 leaves the active binding pocket, in front of PQQ, to get to the solvent, as easily as with a variety of other O2-activating enzymes, O2 carriers, and gas-sensing proteins. The shortest pathway, orthogonal to the center of the mean plane of PQQ, is largely preferred by O2 over pathways slightly deviating from this line. These observations challenge the interpretation of an impermeable active binding pocket of PqqC-PQQ, as drawn from both X-ray diffraction data of the crystal at low temperature and physiological experimentation. Key residues for the minor O2 gates are 1. Q155, L158, R177, and R17, 2. E188, and L191, and 3. D83 and Q182, or the main O2 egress involving residues P151, L180, and A183, modeling, overview
the enzyme has 14 conserved active site residues, which are in close contact with bound substrate pyrroloquinoline quinone. It exhibits a stepwise process in which substrate binding leads to the generation of the closed protein conformation, with the latter playing a critical role in O2 binding and catalysis
physiological function
enzyme Pqq C, encded by gene pqqC, is essential for antifungal activity of Pseudomonas kilonensis JX22 against Fusarium oxysporum f. sp. lycopersici. Strain JX22 shows broad range of antifungal and antibacterial activities to plant pathogens, e.g. it significantly inhibits mycelial growth of Fusarium oxysporum f. sp. lycopersici strain ATCC 9848
physiological function
pyrroloquinoline quinone, i.e. 4,5-dihydro-4,5-dioxo-1Hpyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid, PQQ, synthesized by the enzyme, is a bacterial cofactor in numerous alcohol dehydrogenases including methanol dehydrogenase and glucose dehydrogenase
physiological function
the enzyme is involved in biosynthesis of pyrroloquinoline quinone, PQQ, a cofactor of various membrane-bound dehydrogenases. The amount of endogenous PQQ is generally regarded as a bottleneck to achieving higher catalytic efficiency of PQQ-dependent dehydrogenases. PQQ biosynthesis can be enhanced by overexpressing some of the individual genes in the gene cluster in Gluconobacter oxydans and the PQQ levels are positively correlated with the efficiency of conversion of D-sorbitol to L-sorbose, overexpression of PQQ-related genes activates L-sorbose production and D-sorbitol dehydrogenase activity
Results 1 - 10 of 10