BRENDA - Reference to 2.3.1.B2; Id = 719116

expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates

Pseudomonas sp.

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

-

?

Pseudomonas sp.

-

Pseudomonas sp. 61-3

-

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

?

-

class I PHA synthase

-

Pseudomonas sp.

PHA synthase 1

-

Pseudomonas sp.

polyhydroxyalkanoate synthase

-

Pseudomonas sp.

type I PHA synthase

-

Pseudomonas sp.

expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates

Pseudomonas sp.

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

-

1

-

1

-

1

-

736527

Tai

Discovery of a new polyhydroxy ...

uncultured bacterium, uncultured bacterium SC8

J. Biosci. Bioeng.

121

355-364

2015

-

1

-

6

-

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

-

735855

Foong

Whole genome amplification app ...

Marinobacter sp., Marinobacter sp. C1S70

BMC Microbiol.

14

318

2014

-

2

-

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

-

5

-

1

-

1

-

1

-

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

-

1

-

2

-

736535

Park

Propionyl-CoA dependent biosyn ...

Pseudomonas sp., Pseudomonas sp. MBEL 6–19

J. Biotechnol.

165

93-98

2013

-

1

-

1

-

7

-

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

3

1

-

1

-

1

-

1

2

-

1

-

2

-

2

1

-

1

-

714539

Matsumoto

A new pathway for poly(3-hydro ...

Cupriavidus necator

Biosci. Biotechnol. Biochem.

75

364-366

2011

-

1

-

1

-

1

-

1

-

2

-

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

-

2

-

1

-

2

-

13

-

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

2

-

2

-

1

-

21

-

2

-

1

-

1

-

1

-

2

-

685487

Zhang

Mechanism of the polymerizatio ...

Cupriavidus necator

Biomacromolecules

4

504-509

2003

-

1

-

3

-

1

-

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

-

4

-

1

-

685486

Song

In vitro polymerization and co ...

Cupriavidus necator

Biomacromolecules

1

433-439

2000

-

1

-

1

-

3

-

1

-

2

-

2

-

1

-

1

-

1

-

1

-

1

-

2

-

1

-

687130

Kichise

Biosynthesis of polyhydroxyalk ...

Aeromonas caviae

Int. J. Biol. Macromol.

25

69-77

1999

-

1

-

3

-

1

-

1

-

A new beneficial mutation in Pseudomonas sp. 61-3 polyhydroxyalkanoate (PHA) synthase for enhanced cellular content of 3-hydroxybutyrate-based PHA explored using its enzyme homolog as a mutation template

Data extracted from this reference: