BRENDA - Enzyme Database
show all sequences of 2.3.1.B5

PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo

Sim, S.J.; Snell, K.D.; Hogan, S.A.; Stubbe, J.; Rha, C.; Sinskey, A.J.; Nat. Biotechnol. 15, 63-67 (1997)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer
Cupriavidus necator
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cupriavidus necator
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer
Cupriavidus necator
Other publictions for EC 2.3.1.B5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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735496
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1421-1429
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736277
Gowda
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Poly(3)hydroxybutyrate (PHB) p ...
Bacillus thuringiensis, Bacillus thuringiensis IAM 12077
Int. J. Pharm. Bio Sci.
4
B794-B802
2013
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719032
Tomizawa
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Bacillus cereus, Bacillus cereus YB-4, Bacillus megaterium, Bacillus megaterium NBRC15308
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12
2660-2666
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2
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50
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26
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684934
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Escherichia coli
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374
485-489
2008
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52
209-214
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1
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684663
Hezayen
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Halopiger aswanensis, Halopiger aswanensis DSM 13151
Arch. Biochem. Biophys.
403
284-291
2002
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1
1
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688851
Qi
Polyhydroxybutyrate biosynthes ...
Caulobacter vibrioides
Microbiology
147
3353-3358
2001
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689122
Sim
PHA synthase activity controls ...
Cupriavidus necator
Nat. Biotechnol.
15
63-67
1997
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687271
Wodzinska
-
Polyhydroxybutyrate synthase: ...
Cupriavidus necator
J. Am. Chem. Soc.
118
6319-6320
1996
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