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evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
evolution
-
enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
-
evolution
-
enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
-
evolution
-
enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
-
evolution
-
enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
-
evolution
-
enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
-
evolution
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enzymes from actinobacteria and gammaproteobacteria seem to belong to different subgroups of the mcl PHA depolymerases, sequence comparisons, overview
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malfunction
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a phaZ mutant exhibits increased poly-3-hydroxybutyrate accumulation during free-living growth, even when grown under non-poly-3-hydroxybutyrate -inducing conditions. The phaZ mutant demonstrates no reduction in symbiotic capacity. This mutant also exhibits a decreased capacity to tolerate long-term carbon starvation, comparable to that of other poly-3-hydroxybutyrate cycle mutants. In contrast to other poly-3-hydroxybutyrate cycle mutants, the phaZ mutant does not exhibit any decrease in rhizosphere competitiveness, but it exhibits a significant increase in succinoglycan biosynthesis
malfunction
disruption of the phaZ1 gene significantly affects intracellular poly(3-hydroxybutyrate) mobilization during the poly(3-hydroxybutyrate)-degrading stage in Bacillus megaterium, as demonstrated by transmission electron microscopy and the measurement of the poly(3-hydroxybutyrate) content
malfunction
a phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell
malfunction
a phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell. Cells bearing a phaZ3 knockout are found to have a higher granule count than the wild-type, whereas granule volume per cell volume is similar
malfunction
cells bearing a phaZ2 knockout mutation alone or in conjunction with a phaZ1 mutation are found to have a high granule volume per cell volume and a higher granule count compared to wild-type. A phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell. Cells bearing a phaZ3 knockout are found to have a higher granule count than the wild-type, whereas granule volume per cell volume is similar
malfunction
chromosomal deletion of phaZd1, phaZd2, or both depolymerase genes has no significant effect on PHB accumulation and mobilization during growth in nutrient broth or nutrient broth-gluconate medium
malfunction
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chromosomal deletion of phaZd1, phaZd2, or both depolymerase genes has no significant effect on PHB accumulation and mobilization during growth in nutrient broth or nutrient broth-gluconate medium
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malfunction
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cells bearing a phaZ2 knockout mutation alone or in conjunction with a phaZ1 mutation are found to have a high granule volume per cell volume and a higher granule count compared to wild-type. A phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell. Cells bearing a phaZ3 knockout are found to have a higher granule count than the wild-type, whereas granule volume per cell volume is similar
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malfunction
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a phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell
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malfunction
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a phaZ quadruple knockout strain, lacking genes phaZ1, phaZ2, phaZ3, and phaZ5, appears to have a low granule volume per cell volume and a low granule count per cell. Cells bearing a phaZ3 knockout are found to have a higher granule count than the wild-type, whereas granule volume per cell volume is similar
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physiological function
PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd1 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo
physiological function
PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd2 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo
physiological function
the enzyme has an impact on granule architecture. Overexpression of specific phaZ genes influences polyhydroxybutyrate homeostasis
physiological function
phosphorylations of residues Thr26 and Ser35 of PhaZa1 reduce the ability of Cupravidius necator to mobilize polyhydroxybutanoate in the stationary growth phase
physiological function
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PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd2 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo
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physiological function
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the enzyme has an impact on granule architecture. Overexpression of specific phaZ genes influences polyhydroxybutyrate homeostasis
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physiological function
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PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd1 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo
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additional information
active site Ser190
additional information
active site Ser190
additional information
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active site Ser190
additional information
active site Ser193
additional information
active site Ser193
additional information
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active site Ser193
additional information
five amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme are all located at a single surface-exposed location of the enzyme
additional information
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five amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme are all located at a single surface-exposed location of the enzyme
additional information
the enzyme has a globular shape with an alpha-beta hydrolase fold, three-dimensional structure and homology structure modelling, overview
additional information
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the enzyme has a globular shape with an alpha-beta hydrolase fold, three-dimensional structure and homology structure modelling, overview
additional information
the enzyme has three functional domains to effectively degrade solid poly((R)-3-hydroxybutyrate) materials, and its catalytic domain catalyzes the ester bond cleavage of the substrate
additional information
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the enzyme has a globular shape with an alpha-beta hydrolase fold, three-dimensional structure and homology structure modelling, overview
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additional information
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active site Ser193
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additional information
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active site Ser190
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additional information
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the enzyme has three functional domains to effectively degrade solid poly((R)-3-hydroxybutyrate) materials, and its catalytic domain catalyzes the ester bond cleavage of the substrate
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