Information on EC 2.3.1.B3 - type II polyhydroxybutyrate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
type II polyhydroxybutyrate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n = [(R)-3-hydroxyacyl]n+1 + CoA
show the reaction diagram
specific for medium-chain acyl-CoA with a chain length of 6-14 carbon atoms. The enzyme is composed of a single subunit.
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxybutyrate O-acyltransferase (medium-chain)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
KCTC 1637, gene phaC1Ps6-19
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Manually annotated by BRENDA team
gene phaC1Ps6-19
UniProt
Manually annotated by BRENDA team
gene phaC1Ps6-19
UniProt
Manually annotated by BRENDA team
gene phaC1Ps6-19
UniProt
Manually annotated by BRENDA team
gene phaC1Ps6-19
UniProt
Manually annotated by BRENDA team
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-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
show the reaction diagram
3-hydroxybutyryl-CoA + 3-hydroxyhexanoate
poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) + CoA
show the reaction diagram
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3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
show the reaction diagram
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?
3-hydroxybutyryl-CoA + 3-hydroxyvaleryl-CoA
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
show the reaction diagram
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?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
show the reaction diagram
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mutant enzymes
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
show the reaction diagram
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?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[3-hydroxybutyrate](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-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
show the reaction diagram
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PhaC1Pp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; While Chromobacterium violaceum accumulates poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) when grown on a fatty acid carbon source, Klebsiella aerogenes and Ralstonia eutropha (formerly Alcaligenes eutrophus), harboring phaCCv, accumulate poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) and, additionally, poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) when even-chain-length fatty acids are utilized as the carbon source. This finding suggests that the metabolic environments of these organisms are sufficiently different to alter the product range of the Chromobacterium violaceum PHA synthase. Neither recombinant Escherichia coli nor recombinant Pseudomonas putida harboring phaCCv accumulate significant levels of polyhydroxyalkanoic acids
expression in Pseudomonas putida GPp104 PHA mutant
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expression of wild-type and mutant enzymes in Escherichai coli altering its content of polyhydroxyalkanoates
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gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
gene phaC1Ps6-19, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of mutant E130D/S325T/S477G/Q481K in Escherichia coli strain XL-1 Blue
mutant enzymes expressed in Escherichia coli
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recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase
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recombinant expression of His-tagged PhaC1Pp in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E130D/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S477F/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
A547V
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mutation increases polyhydroxyalkanoate yields
E130D/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S477F/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
L484V
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mutation remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis
Q481M
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mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
S482G
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mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
A547V
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mutation increases polyhydroxyalkanoate yields
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L484V
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mutation remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis
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Q481M
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mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
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S482G
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mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
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E130D/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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E130D/S325T/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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E130D/S325T/S477G/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
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E130D/S477F/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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E115K/S325C
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highly enhanced synthesis of poly(3-hydroxybutyrate)
E130D
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recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. Mutation results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. In vitro enzyme activities of the E130D PHA synthase toward various 3-hydroxyacyl-CoAs (4-10 carbons in length) are all higher than those of the wild-type enzyme. Mutation decreases the molecular weight of poly(3-hydroxybutyrate)
E130D/Q481K
E130D/Q481M
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the double mutant shows much higher poly(3-hydroxybutyrate) accumulation (29-34 wt%) compared to poly(3-hydroxybutyrate) accumulation in cells harboring PHA synthase with the individual mutations E130D or Q481M alone
E130D/Q481R
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the double mutant shows much higher poly(3-hydroxybutyrate) accumulation (29-34 wt%) compared to poly(3-hydroxybutyrate) accumulation in cells harboring PHA synthase with the individual mutations E130D or Q481R alone
E130D/S325C
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the double mutants of E130D with either the S325T or the S325C mutations exhibits strong synergistic increases in poly(3-hydroxybutyrate) content, up to 39 wt%
E130D/S325T
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the double mutants of E130D with either the S325T or the S325C mutations exhibits strong synergistic increases in poly(3-hydroxybutyrate) content, up to 39 wt%
E130D/S325T/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
L20P/Q481R
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highly enhanced synthesis of poly(3-hydroxybutyrate)
N16T/M292V/S325T
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highly enhanced synthesis of poly(3-hydroxybutyrate)
N5D/Q481K
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highly enhanced synthesis of poly(3-hydroxybutyrate)
Q481K/Q508L
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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
Q481M/Q508L
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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
Q481R/Q508L
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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
Q508L
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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
S325C
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highly enhanced synthesis of poly(3-hydroxybutyrate)
S325C/H350T
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highly enhanced synthesis of poly(3-hydroxybutyrate)
S325T/Q481K
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S325T mutation decreases the molecular weight of poly(3-hydroxybutyrate). If the mutation is combined with the Q481K mutation, the enzyme can produce poly(3-hydroxybutyrate) with higher molecular weight
S325T/Q508L
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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
S477R
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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
S477R/Q508L
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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
E130D
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recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. Mutation results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. In vitro enzyme activities of the E130D PHA synthase toward various 3-hydroxyacyl-CoAs (4-10 carbons in length) are all higher than those of the wild-type enzyme. Mutation decreases the molecular weight of poly(3-hydroxybutyrate)
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E130D/Q481K
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E130D mutation decreases the molecular weight of poly(3-hydroxybutyrate). If the mutation is combined with the Q481K mutation, the enzyme can produce poly(3-hydroxybutyrate) with higher molecular weight; site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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E130D/S325T/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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E130D/S325T/S477G/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA); site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
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E130D/S477F/Q481K
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site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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Q481K
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highly enhanced synthesis of poly(3-hydroxybutyrate); mutation decreases the molecular weight of poly(3-hydroxybutyrate)
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Q481M
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highly enhanced synthesis of poly(3-hydroxybutyrate)
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Q481R
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highly enhanced synthesis of poly(3-hydroxybutyrate)
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S325C
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highly enhanced synthesis of poly(3-hydroxybutyrate)
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S325T
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highly enhanced synthesis of poly(3-hydroxybutyrate); mutation decreases the molecular weight of poly(3-hydroxybutyrate)
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S325T/Q481K
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S325T mutation decreases the molecular weight of poly(3-hydroxybutyrate). If the mutation is combined with the Q481K mutation, the enzyme can produce poly(3-hydroxybutyrate) with higher molecular weight
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis