Information on EC 2.3.1.B5 - unclassified polyhydroxybutyrate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.3.1.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
unclassified polyhydroxybutyrate synthase
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:3-hydroxybutyrate O-acyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
a PHA-producing strain isolated from a soil sample from western peninsular Malaysia, gene phaCUSMAA2-4
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Manually annotated by BRENDA team
a PHA-producing strain isolated from a soil sample from western peninsular Malaysia, gene phaCUSMAA2-4
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
isolated in Malaysia, gene phbC encoded in the phb operon
UniProt
Manually annotated by BRENDA team
isolated in Malaysia, gene phbC encoded in the phb operon
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
show the reaction diagram
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
show the reaction diagram
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
show the reaction diagram
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acylation of C319 causes a shift of the monomeric form of the synthase to its dimeric form, and this shift is accompanied by a substantial increase in its specific activity and a substantial decrease in the lag phase of polymer formation
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?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
show the reaction diagram
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
show the reaction diagram
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-
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?
3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
show the reaction diagram
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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optimal activity at 100 mM
Mg2+
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addition of Mg2+ shows the strongest activation effect. However, high enzyme activity without Mg2+ ions is observed, when other ions are present, suggesting that Mg2+ ions do not serve as cofactors
additional information
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in the absence of salts the granule-bound PHB synthase still exhibits about 40% of the maximum activity. Enzyme activity is strongly enhanced by slightly increasing the ionic strength independent of the salt
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl phosphate
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activates the enzyme and the level of activation is dependent on the concentration of acetyl phosphate supplementation
additional information
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upion growth in in N2 deficient medium, cell biomass remains almost steady from 0 h after transfer to production medium till the end of fermentation (120 h), while polyhydroxybutanoate yield shows an increase from 0.533 g/l at 0 h to 4g/l by 48 h and later gradually decreases, with increase in polyhydroxybutanoate accumulation increase from 11% to 77% by 96 h
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056
(R)-3-hydroxybutyryl-CoA
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0.0802 - 0.14
3-hydroxybutyryl-CoA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
CoA
Halopiger aswanensis
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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193259 cpm/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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pH 6.5: about 30% of maximal activity, pH 8.5: about 85% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
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20°C: about 50% of maximal activity, 70°C: about 50% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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expression in Escherichia coli
D2Z0B8 and D2Z0B6
expression of PhaRCBm, and as hybrid enzyme PhaRYB4CBm with Bacillus cereus YB-4, PhaRCYB4 in Escherichia coli JM109
expression of PhaRCYB4, and as hybrid enzyme PhaRYB4CBm with Bacillus megaterium NBRC15308, PhaRCBm in Escherichia coli JM109
gene phaCUSMAA2-4, DNA and amino acid sequence determination and analysis, expression in and complementation of mutant Cupriavidus necator PHB-4 deficient in PHA synthesis, expression in Escherichia coli strain S17-1
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gene phbCPs encoded in the phb operon, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, the genetic organization of phb operon shows a putative promoter region, followed by phbBPs-phbAPs-phbCPs, with phbRPs encoding a putative transcriptional activator that is located in the opposite orientation, upstream of phbBACPs. Heterologous expression of phbCPs from pGEM3ABex vector in Escherichia coli JM109 resulting in P(3HB) accumulation of up to 40% of dry cell weight
the phaC coding region is subcloned into vector pBBR1-JO2 under lac promoter control. The resulting plasmid, pQQ4, mediates PHB accumulation in the mutant Ralstonia eutropha PHBN4 and recombinant Escherichia coli JM109(pBHR69)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis