Q481K
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481K/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481M
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481M/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481R
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481R/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S325T
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S325T/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S477R
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S477R/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Pseudomonas sp.
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Pseudomonas sp. 61-3
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
719116
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
mutant enzymes
719116
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
mutant enzymes
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
719116
Pseudomonas sp.
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxybutanoate]n+1 + CoA
?
additional information
the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
719116
Pseudomonas sp.
?
additional information
the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
719116
Pseudomonas sp. 61-3
?
Q481K
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481K/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481M
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481M/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481R
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q481R/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S325T
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S325T/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S477R
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
S477R/Q508L
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Pseudomonas sp.
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Pseudomonas sp.
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Pseudomonas sp. 61-3
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
719116
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
mutant enzymes
719116
Pseudomonas sp.
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
mutant enzymes
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxyacyl]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
719116
Pseudomonas sp.
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
719116
Pseudomonas sp. 61-3
[(R)-3-hydroxybutanoate]n+1 + CoA
?
additional information
the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
719116
Pseudomonas sp.
?
additional information
the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
719116
Pseudomonas sp. 61-3
?
735683
Buckley
Chemistry with an artificial p ...
Caulobacter vibrioides
Biochemistry
54
2117-2125
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
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1
-
1
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736527
Tai
Discovery of a new polyhydroxy ...
uncultured bacterium, uncultured bacterium SC8
J. Biosci. Bioeng.
121
355-364
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
735350
Zhang
Mechanistic insight with HBCH2 ...
Cupriavidus necator
ACS Chem. Biol.
9
1773-1779
2014
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
735855
Foong
Whole genome amplification app ...
Marinobacter sp., Marinobacter sp. C1S70
BMC Microbiol.
14
318
2014
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
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1
-
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-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
735485
Thomson
Efficient production of active ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Appl. Environ. Microbiol.
79
1948-1955
2013
-
1
1
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
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-
-
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
735535
Ochi
Engineering of class i lactate ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Appl. Microbiol. Biotechnol.
97
3441-3447
2013
-
1
-
-
2
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
1
-
-
-
2
-
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-
-
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-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736535
Park
Propionyl-CoA dependent biosyn ...
Pseudomonas sp., Pseudomonas sp. MBEL 6–19
J. Biotechnol.
165
93-98
2013
-
1
1
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
718922
Cho
Purification of polyhydroxybut ...
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Biochemistry
51
2276-2288
2012
-
-
1
-
1
-
-
-
-
-
1
2
-
42
-
-
1
-
-
-
2
-
2
2
3
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
1
2
-
-
-
1
-
-
2
-
2
2
1
-
-
-
-
-
-
-
-
1
1
-
-
-
714539
Matsumoto
A new pathway for poly(3-hydro ...
Cupriavidus necator
Biosci. Biotechnol. Biochem.
75
364-366
2011
-
1
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
719116
Shozui
A new beneficial mutation in P ...
Pseudomonas sp., Pseudomonas sp. 61-3
Biosci. Biotechnol. Biochem.
74
1710-1712
2010
-
-
1
-
11
-
-
-
-
-
-
4
-
6
-
-
-
-
-
-
-
-
8
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
11
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684590
Zheng
Mutation on N-terminus of poly ...
Cupriavidus necator
Appl. Microbiol. Biotechnol.
72
896-905
2006
-
-
-
-
13
-
-
-
-
-
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-
-
2
-
-
-
-
-
-
-
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1
-
2
-
-
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-
13
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685489
Matsumoto
Enhancement of poly(3-hydroxyb ...
Aeromonas caviae
Biomacromolecules
6
2126-2130
2005
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685729
Normi
Site-directed saturation mutag ...
Cupriavidus necator
Biotechnol. Lett.
27
705-712
2005
-
-
-
-
19
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
19
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688783
Normi
Characterization and propertie ...
Cupriavidus necator
Macromol. Biosci.
5
197-206
2005
-
-
1
-
21
-
-
2
-
-
1
-
-
3
-
-
1
-
-
-
-
-
1
1
2
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
21
-
-
-
-
2
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
685487
Zhang
Mechanism of the polymerizatio ...
Cupriavidus necator
Biomacromolecules
4
504-509
2003
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685312
Rehm
Molecular characterization of ...
Cupriavidus necator
Biochim. Biophys. Acta
1594
178-190
2002
-
-
1
-
11
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684662
Yuan
Class I and III polyhydroxyalk ...
Cupriavidus necator
Arch. Biochem. Biophys.
394
87-98
2001
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685059
Jia
Mechanistic studies on class I ...
Cupriavidus necator
Biochemistry
40
1011-1019
2001
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685486
Song
In vitro polymerization and co ...
Cupriavidus necator
Biomacromolecules
1
433-439
2000
-
-
1
-
-
-
1
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
2
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
-
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687130
Kichise
Biosynthesis of polyhydroxyalk ...
Aeromonas caviae
Int. J. Biol. Macromol.
25
69-77
1999
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