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S102A
-
mutant without poly[(R)-3-hydroxybutanoate]n hydrolyzing activity
C178A
-
no degradation of amorphous poly(3-hydroxybutyrate) granules or 3-hydroxybutyrate oligomers
S190A
site-directed mutagenesis, inactive mutant
S193A
site-directed mutagenesis, inactive mutant
S190A
-
site-directed mutagenesis, inactive mutant
-
S193A
-
site-directed mutagenesis, inactive mutant
-
A134G
-
PHB depolymerase activity similar to wild type
A134G, H135L
-
PHB depolymerase activity similar to wild type, 2fold lipase activity compared to wild type
D242A
-
no PHB depolymerase activity
D242N
-
no PHB depolymerase activity
D256A
-
PHB depolymerase activity similar to wild type
D256N
-
PHB depolymerase activity similar to wild type
F198E
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
F251E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F9E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F9E/S136A
site-directed mutagenesis, inactive mutant
H306A
-
no PHB depolymerase activity
H47A
-
no PHB depolymerase activity
INPNC-PhaZ1
fusion protein
INPNC-PhaZ1-INPNC-PrePhaZ1 fusion construct
does not affect growth of host cells
INPNC-PrePhaZ1
fusion protein
PhaZ1-PrePhaZ1 fusion construct
construct containing PhaZ1 and its own N-terminal signal peptide (PrePhaZ1) enables the secretion of active PhaZ1 into the extracellular medium
PrePhaZ1
N-terminal signal peptide
S136A/?W202-V208
site-directed mutagenesis, inactive mutant
S136A/W207E
site-directed mutagenesis, inactive mutant
S136A/W252E
site-directed mutagenesis, inactive mutant
S136A/Y176E
site-directed mutagenesis, inactive mutant
S136A/Y189E
site-directed mutagenesis, inactive mutant
S136A/Y190E
site-directed mutagenesis, inactive mutant
S136T
-
20% PHB depolymerase activity
W202-V208
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W207E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W252E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y103A
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Y103E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E/S136A
site-directed mutagenesis, inactive mutant
Y105E/S136A/Y189E
site-directed mutagenesis, inactive mutant, no substrate binding
Y105E/S136A/Y190E
site-directed mutagenesis, inactive mutant, no substrate binding
Y105F
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Y124E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y169E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y172A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y173S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y176E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y189A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y190A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y203S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y204S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y66E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y66E/S136A
site-directed mutagenesis, inactive mutant
KTMQ01
-
phaZ knockout mutant, Pseudomonas putida KTMQ01
A66V
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/N251S/T290A
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/N285D/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/T145S/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
G108G/Q125L/R230R/K260M/T284S/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285A
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285E
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285G
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285H
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
S445C
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. S445C has higher poly((R)-3-hydroxybutyrate)-degrading activity than wild-type. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
S92S/G180D/I292F
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
S92S/T145S/N285Y
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T145S/S246T/T252T/S257T
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T252T/S257T/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T37A/C51C/N285Y
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T37A/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
Y443H
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
A66V
-
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
L441H
-
mutant enzyme with lower degradation of denatured poly(R)-3-hydroxybutyrate and adsorption abilities. Lowering the affinity of the substrate-binding domain towards denatured poly(R)-3-hydroxybutyrate causes a decrease in the degradation rate without the loss of its hydrolytic activity for the polymer chain
-
N285A
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285D/G310G
-
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
N285G
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285Y
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
T37A/C51C/N285Y
-
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
D209N
site-directed mutagenesis, inactive mutant
H269E
site-directed mutagenesis, inactive mutant
H269Q
site-directed mutagenesis, inactive mutant
S131A
site-directed mutagenesis, inactive mutant
S131C
site-directed mutagenesis, inactive mutant
D209N
-
site-directed mutagenesis, inactive mutant
-
H269E
-
site-directed mutagenesis, inactive mutant
-
H269Q
-
site-directed mutagenesis, inactive mutant
-
S131A
-
site-directed mutagenesis, inactive mutant
-
S131C
-
site-directed mutagenesis, inactive mutant
-
S39A
-
inactive mutant, pdb accession code 2D81
S136A
-
no PHB depolymerase activity
S136A
site-directed mutagenesis, active site mutation, inactive mutant
Y105E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y105E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E
mutant displays reduced binding to olyhydroxybutanoate
Y105E/Y189E
site-directed mutagenesis
Y105E/Y189E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E/Y190E
site-directed mutagenesis
Y105E/Y190E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y189E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y189E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y190E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y190E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L441H
mutant enzyme with lower degradation of denatured poly(R)-3-hydroxybutyrate and adsorption abilities. Lowering the affinity of the substrate-binding domain towards denatured poly(R)-3-hydroxybutyrate causes a decrease in the degradation rate without the loss of its hydrolytic activity for the polymer chain
L441H
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
N285D
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D
site-directed mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285Y
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285Y
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285D
-
site-directed mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
additional information
-
construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
deletion of phaZd1 without effect on enzyme activity
additional information
deletion of phaZd1 without effect on enzyme activity
additional information
-
deletion of phaZd1 without effect on enzyme activity
additional information
deletion of phaZd2 without effect on enzyme activity
additional information
deletion of phaZd2 without effect on enzyme activity
additional information
-
deletion of phaZd2 without effect on enzyme activity
additional information
generation of a set of phaZ gene deletion strains, i.e. DELTAphaZ1, DELTAphaZ2, DELTAphaZ3, DELTAphaZ1DELTAphaZ2, DELTAphaZ1DELTAphaZ3, DELTAphaZ2DELTAphaZ3, and DELTAphaZ1DELTAphaZ2DELTAphaZ3 from strain H16. All mutant strains are unable to produce poly(hydroxybutyrate)
additional information
-
generation of a set of phaZ gene deletion strains, i.e. DELTAphaZ1, DELTAphaZ2, DELTAphaZ3, DELTAphaZ1DELTAphaZ2, DELTAphaZ1DELTAphaZ3, DELTAphaZ2DELTAphaZ3, and DELTAphaZ1DELTAphaZ2DELTAphaZ3 from strain H16. All mutant strains are unable to produce poly(hydroxybutyrate)
additional information
recombinant Cupriavidus necator strain KNK-005 harbors an NSDG mutant of the PHA synthase gene (phaCAc) from Aeromonas caviae. Deletion of phaZ1 and phaZ2 (EC 3.1.1.22, UniProt ID Q0K7T2) has a significant and slight attenuating effect, respectively, on the reduction in polyhydroxyalkanoate (PHA) content of KNK-005 cells. Regardless of the PHA consumption, its molecular weight does not decrease. The DELTAphaZ1DELTAphaZ2DELTAphaZ6 triple mutant of KNK-005, 005dZ126, is a promising strain capable of producing ultra-high-molecular-weight poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBHHx) of ultra-high-molecular-weight and barely degrades PHBHHx and polyhydroxyalkanoate enzymatically intracellularly
additional information
-
recombinant Cupriavidus necator strain KNK-005 harbors an NSDG mutant of the PHA synthase gene (phaCAc) from Aeromonas caviae. Deletion of phaZ1 and phaZ2 (EC 3.1.1.22, UniProt ID Q0K7T2) has a significant and slight attenuating effect, respectively, on the reduction in polyhydroxyalkanoate (PHA) content of KNK-005 cells. Regardless of the PHA consumption, its molecular weight does not decrease. The DELTAphaZ1DELTAphaZ2DELTAphaZ6 triple mutant of KNK-005, 005dZ126, is a promising strain capable of producing ultra-high-molecular-weight poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBHHx) of ultra-high-molecular-weight and barely degrades PHBHHx and polyhydroxyalkanoate enzymatically intracellularly
additional information
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deletion of phaZd2 without effect on enzyme activity
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants
-
additional information
-
deletion of phaZd1 without effect on enzyme activity
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
-
additional information
-
GST-catalytic domain fusion protein, high binding capacity on single crystals of poly(3-hydroxybutyrate)
additional information
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construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
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C-terminal truncation, poly(3-hydroxybutyrate)-specific binding domain within the C-terminus
additional information
construction of a PhaZ7 variant with deletion of residues 202-208. Exchange of surface-exposed amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme, by less hydrophobic, hydrophilic or negatively charged residues reduces binding of the enzyme to substrate poly(3-hydroxybutyrate). Modifications of other residues at the enzyme surface, i.e. F9, Y66, Y103, Y124, Y169, Y172, Y173, F198, Y203, Y204, F251, and W252, have no effect on substrate binding
additional information
-
construction of a PhaZ7 variant with deletion of residues 202-208. Exchange of surface-exposed amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme, by less hydrophobic, hydrophilic or negatively charged residues reduces binding of the enzyme to substrate poly(3-hydroxybutyrate). Modifications of other residues at the enzyme surface, i.e. F9, Y66, Y103, Y124, Y169, Y172, Y173, F198, Y203, Y204, F251, and W252, have no effect on substrate binding
additional information
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construction of several GST-fusion domains, analysis of substrate-binding domains
additional information
-
construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
N17-mutant unable to degrade poly(3-hydroxybutyrate), obtained with the random insertion of a minitransposon, Tn5. Mutant accumulates the poly(3-hydroxybutyrate) depolymerase in the periplasm and cytoplasm, and does not secrete the enzyme into the external medium
additional information
mutated phaZRpiT1 genes generated by error-prone PCR are fused to the oprI gene from Pseudomonas aeruginosa to display them as anchored fusion proteins on Escherichia coli cell surface, screening for activity with 4-nitrophenyl butyrate. The wholecell catalysis is a promising and suitable tool to screen for PHB depolymerases with enhanced catalytic activity
additional information
the poly((R)-3-hydroxybutyrate)-degrading activities of N285X are reciprocally related to their pNPCn-hydrolyzing activities, with the exception of N285A and N285G, and that His residue could functionally substitute for Asn285 on poly((R)-3-hydroxybutyrate) degradation. Among the mutant enzymes, N285E displays the highest hydrolysis rate regardless of substrate concentration or carbon chain length. N285A has comparable hydrolysis rates to N285E at low substrate concentrations (0.1-0.4 mM) for all the substrates regardless of carbon chain lengths. N285H shows one of the lowest hydrolysis rates among the mutant enzymes regardless of substrate concentration or carbon chain length
additional information
-
the poly((R)-3-hydroxybutyrate)-degrading activities of N285X are reciprocally related to their pNPCn-hydrolyzing activities, with the exception of N285A and N285G, and that His residue could functionally substitute for Asn285 on poly((R)-3-hydroxybutyrate) degradation. Among the mutant enzymes, N285E displays the highest hydrolysis rate regardless of substrate concentration or carbon chain length. N285A has comparable hydrolysis rates to N285E at low substrate concentrations (0.1-0.4 mM) for all the substrates regardless of carbon chain lengths. N285H shows one of the lowest hydrolysis rates among the mutant enzymes regardless of substrate concentration or carbon chain length
-
additional information
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N17-mutant unable to degrade poly(3-hydroxybutyrate), obtained with the random insertion of a minitransposon, Tn5. Mutant accumulates the poly(3-hydroxybutyrate) depolymerase in the periplasm and cytoplasm, and does not secrete the enzyme into the external medium
-
additional information
-
mutated phaZRpiT1 genes generated by error-prone PCR are fused to the oprI gene from Pseudomonas aeruginosa to display them as anchored fusion proteins on Escherichia coli cell surface, screening for activity with 4-nitrophenyl butyrate. The wholecell catalysis is a promising and suitable tool to screen for PHB depolymerases with enhanced catalytic activity
-