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3.1.1.75: poly(3-hydroxybutyrate) depolymerase

This is an abbreviated version!
For detailed information about poly(3-hydroxybutyrate) depolymerase, go to the full flat file.

Word Map on EC 3.1.1.75

Reaction

[(R)-3-hydroxybutanoate]n
+
H2O
=
[(R)-3-hydroxybutanoate]n-x
+
[(R)-3-hydroxybutanoate]x

Synonyms

AFUA_4G03560, i-PHA depolymerase, intracellular poly(3-hydroxybutyrate) depolymerase, intracellular poly(3-hydroybutyrate) depolymerase, MCL-PHA depolymerase, medium chain length polyhydroxyalkanoate depolymerase, P(3HB) depolymerase, P(3HB) depolymerase A, P(3HB) depolymerase B, P(3HB-co-3HV) depolymerase, P(3HV) depolymerase, PDI, PHA depolymerase, PHAase I, PHAase II, PhaZ, PhaZ-Th, PhaZ1, PhaZ1-Z6, phaZ3, PhaZ5, PhaZ6, PhaZ7, PhaZ7 depolymerase, PhaZa1, PhaZBm, PhaZd, PhaZd1, PhaZd2, PhaZRpiT1, PhaZSa, PHB depolymerase, PHB depolymerase A, PHB depolymerase inhibitor, PHB-depolymerase, PHBDP, PHV depolymerase, poly (beta-hydroxybutyrate) depolymerase, poly(3-hydroxybutyrate) (PHB) depolymerase, poly(3-hydroxybutyrate) depolymerase, poly(3-hydroxyvalerate) depolymerase, poly(3-hydroxyvaleric acid) depolymerase, poly(3HB) depolymerase, poly(beta-hydroxybutyrate) depolymerase, poly(HA SCL) depolymerase, poly(HA) depolymerase, poly(hydroxybutyric) depolymerase, poly-beta-hydroxybutyrate depolymerase, poly-beta-hydroxybutyric acid depolymerase, polyhydroxyalkanoate depolymerase, polyhydroxybutyrate depolymerase, poly[(R)-3-hydroxybutyrate] depolymerase, poly[(R)-hydroxyalkanoic acid] depolymerase, poly[D(-)-3-hydroxybutyrate] depolymerase

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.75 poly(3-hydroxybutyrate) depolymerase

Engineering

Engineering on EC 3.1.1.75 - poly(3-hydroxybutyrate) depolymerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis, inactive mutant
-
S193A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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
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
S136C
-
no expression
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
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
Y105E/Y189E
Y105E/Y190E
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
Y189E
Y190A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y190E
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
L441H
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
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
N285Y
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
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
additional information