Data extracted from this reference:
Cloned(Commentary)
construction of an N-terminally Strep2-tagged PhaC, Strep2-PhaCRe, and integration into the Ralstonia eutropha genome in place of wild-type phaC and functional expression without a lag phase of CoA release in the enzyme reaction, functional expression of Strep2-PhaCRe in Escherichia coli strain BL21(DE3) showing a lag phase in CoA release
Cupriavidus necator
Engineering
C319A
site-directed mutagenesis
Cupriavidus necator
Molecular Weight [Da]
64000
1 * 64000, PhaC, SDS-PAGE; 2 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
Natural Substrates/ Products (Substrates)
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Cupriavidus necator
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
[(R)-3-hydroxybutanoate]n+1 + CoA
?
Organism
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Purification (Commentary)
recombinant N-terminally Strep2-tagged PhaC from Ralstonia eutropha by affinity chromatography. Strep2-PhaCRe co-purifies with the phasin protein, PhaP1, and with soluble polyhydroxybutyrate of 350 kDa MW in a high-molecular weight complex and in monomeric/dimeric forms with no associated PhaP1 or polyhydroxybutyrate
Cupriavidus necator
Specific Activity [micromol/min/mg]
3
8
pooled monomeric and dimeric fractions of Strep2-PhaCRe, 30°C, pH not specified in the publication
Cupriavidus necator
36
purified recombinant Strep2-PhaCRe, 30°C, pH not specified in the publication
Cupriavidus necator
Substrates and Products (Substrate)
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
718922
Cupriavidus necator
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
718922
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
[(R)-3-hydroxybutanoate]n+1 + CoA
?
Subunits
dimer
2 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
monomer
1 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
Synonyms
class I PHB synthase
Cupriavidus necator
class I polyhydroxybutyrate synthase
Cupriavidus necator
Temperature Optimum [°C]
30
assay at
Cupriavidus necator
Cloned(Commentary) (protein specific)
construction of an N-terminally Strep2-tagged PhaC, Strep2-PhaCRe, and integration into the Ralstonia eutropha genome in place of wild-type phaC and functional expression without a lag phase of CoA release in the enzyme reaction, functional expression of Strep2-PhaCRe in Escherichia coli strain BL21(DE3) showing a lag phase in CoA release
Cupriavidus necator
Engineering (protein specific)
C319A
site-directed mutagenesis
Cupriavidus necator
Molecular Weight [Da] (protein specific)
64000
1 * 64000, PhaC, SDS-PAGE; 2 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
Natural Substrates/ Products (Substrates) (protein specific)
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Cupriavidus necator
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
[(R)-3-hydroxybutanoate]n+1 + CoA
?
Purification (Commentary) (protein specific)
recombinant N-terminally Strep2-tagged PhaC from Ralstonia eutropha by affinity chromatography. Strep2-PhaCRe co-purifies with the phasin protein, PhaP1, and with soluble polyhydroxybutyrate of 350 kDa MW in a high-molecular weight complex and in monomeric/dimeric forms with no associated PhaP1 or polyhydroxybutyrate
Cupriavidus necator
Specific Activity [micromol/min/mg] (protein specific)
3
8
pooled monomeric and dimeric fractions of Strep2-PhaCRe, 30°C, pH not specified in the publication
Cupriavidus necator
36
purified recombinant Strep2-PhaCRe, 30°C, pH not specified in the publication
Cupriavidus necator
Substrates and Products (Substrate) (protein specific)
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
718922
Cupriavidus necator
[(R)-3-hydroxybutanoate]n+1 + CoA
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
718922
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
[(R)-3-hydroxybutanoate]n+1 + CoA
?
Subunits (protein specific)
dimer
2 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
monomer
1 * 64000, PhaC, SDS-PAGE
Cupriavidus necator
Temperature Optimum [°C] (protein specific)
30
assay at
Cupriavidus necator
General Information
physiological function
class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
Cupriavidus necator
General Information (protein specific)
physiological function
class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
Cupriavidus necator
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2276-2288
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1
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685489
Matsumoto
Enhancement of poly(3-hydroxyb ...
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Biomacromolecules
6
2126-2130
2005
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1
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6
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685729
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Site-directed saturation mutag ...
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Biotechnol. Lett.
27
705-712
2005
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19
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688783
Normi
Characterization and propertie ...
Cupriavidus necator
Macromol. Biosci.
5
197-206
2005
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1
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21
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21
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685487
Zhang
Mechanism of the polymerizatio ...
Cupriavidus necator
Biomacromolecules
4
504-509
2003
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1
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-
1
1
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685312
Rehm
Molecular characterization of ...
Cupriavidus necator
Biochim. Biophys. Acta
1594
178-190
2002
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11
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684662
Yuan
Class I and III polyhydroxyalk ...
Cupriavidus necator
Arch. Biochem. Biophys.
394
87-98
2001
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1
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685059
Jia
Mechanistic studies on class I ...
Cupriavidus necator
Biochemistry
40
1011-1019
2001
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4
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685486
Song
In vitro polymerization and co ...
Cupriavidus necator
Biomacromolecules
1
433-439
2000
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687130
Kichise
Biosynthesis of polyhydroxyalk ...
Aeromonas caviae
Int. J. Biol. Macromol.
25
69-77
1999
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