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2.3.1.304: poly[(R)-3-hydroxyalkanoate] polymerase

This is an abbreviated version!
For detailed information about poly[(R)-3-hydroxyalkanoate] polymerase, go to the full flat file.

Word Map on EC 2.3.1.304

Reaction

(3R)-3-hydroxyacyl-CoA
+
poly[(R)-3-hydroxyalkanoate]n
=
CoA
 +
poly[(R)-3-hydroxyalkanoate]n+1

Synonyms

BP-M-CPF4, broad-range class I PhaCAc, CLAOCE_21140, CLAOCE_21150, CLAOCE_21150/21140, class I PHA synthase, Class I PhaC, class I PhaCRe, class I PHB synthase, Class I poly(R)-hydroxyalkanoic acid synthase, class I polyhydroxyalkanoate synthase, class I polyhydroxybutyrate synthase, Class I synthase, Class II PHA polymerizing enzyme, class II PHA synthase, Class II PhaC, class II PhaC1, class III PHA synthase, class III PHB synthase, class III polyhydroxyalkanoate synthase, class III polyhydroxybutyrate synthase, class III synthase, class IV PHA synthase, H16_A1437, HPTL0263, HPTL0635, HPTL1376, intracellular polyhydroxyalkanoate synthase, P(3HB) synthase, PHA polymerase, PHA synthase, PHA synthase 1, PHA synthase I, PHA synthase II, PHA synthase III, PhaC, PhaC type II, PhaC-II, PhaC1, PhaC1P-5, PhaC1Pp, PhaC1Ps, PhaC1SG, PhaC2, PhaC2P-5, PhaC2Ps, PhaC2SG, PhaCAc, PhaCAv, phaCBP-M-CPF4, PhaCCc, PhaCCn-CAT, PhaCCs, PhaCCs-CAT, phaCCv, PhaCPhaEAv, PhaCRe, PhaE, PhaEC, PhaECAv, PhaRCBm, PhaRCYB4, PHB synthase, PhbC, PhbCRe, phbC_2, phbE, poly(3-hydroxybutyrate) synthase, poly(hydroxyalkanoic acid) synthase, poly-3-hydroxybutyrate synthase, poly-beta-hydroxybutyrate synthase, polyhydroxyalkanoate (PHA) synthase, polyhydroxyalkanoate synthase, polyhydroxyalkanoate synthase 1, polyhydroxyalkanoate synthase synthase, polyhydroxyalkanoic acids synthase, polyhydroxyalkanoic synthase I, polyhydroxyalkanoic synthase II, polyhydroxyalkanoic synthase III, polyhydroxybutyrate synthase, Q667_12980, TH-1_PHB synthase_HPTL_0263, TH-1_PHB synthase_HPTL_0635, TH-1_PHB synthase_HPTL_1376, type I PHA synthase, type I polyhydroxyalkanoate synthase, type II PHA synthase, type II PhaC1, type II polyhydroxyalkanoate synthase, type II Pseudomonas PHA synthase 1, type III PHA synthase, type-III PHA synthase, YdcS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.304 poly[(R)-3-hydroxyalkanoate] polymerase

Engineering

Engineering on EC 2.3.1.304 - poly[(R)-3-hydroxyalkanoate] polymerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D171G
-
the mutation leads to an 8-10fold increase in polyhydroxyalkanoate content in the T1 transgenic Arabidopsis thaliana, compared to plants harboring the wild type enzyme gene
D459V/A513C
-
the mutant shows a 1.1fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 26% as compared with the wild type enzyme
F326I/F518I
-
the mutant shows a 1.06fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 11% as compared with the wild type enzyme
F362I/F518I
-
the double mutation of Phe362Ile and Phe518Ile of PhaCAc causes a 6% increment in the specific synthase activity and an 11% increment of PHA accumulation compared to wild-type synthase
F518I
N149S
-
the mutation leads to an 8-10fold increase in polyhydroxyalkanoate content in the T1 transgenic Arabidopsis thaliana, compared to plants harboring the wild type enzyme gene
S103C/F518I
-
the mutant shows a decrease in specific enzyme activity (to 74%) and polyhydroxyalkanoate accumulation decreases by 45% as compared with the wild type enzyme
V214G
-
the mutant shows a 2.16fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 7% as compared with the wild type enzyme
C130A
C130S
-
121% of wild-type activity in the initial phase of reaction, 16% of wild-type activity in tghe second phase of reaction
C149A
-
inactive mutant protein of PhaC
C149S
-
0.1% of wild-type activity in the initial phase of reaction, 0.09% of wild-type activity in tghe second phase of reaction
c149S/H331Q
-
no activity
C292A
-
mutant of PhaC with wild-type activity
D302A
-
incubation of D302A-PhaCPhaE with [14C]-hydroxybutanoyl-CoA results in detection of oligomeric HBs covalently bound to PhaC, at hydroxybutanoyl-CoA to enzyme ratios between 5 and 100
D302N
-
0.012% of wild-type activity in the initial phase of reaction, 0.29% of wild-type activity in tghe second phase of reaction
H303Q
-
0.25% of wild-type activity in the initial phase of reaction, 1.6% of wild-type activity in tghe second phase of reaction
H331Q
-
51% of wild-type activity in the initial phase of reaction, 73% of wild-type activity in tghe second phase of reaction
A479S
A372_C382del
-
no detectable activity
A510S
mutant is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
A510X
mutation corresponds to position 481 in the class II lactate polymerizing polyhydroxyalkanoate synthase PhaC1PsSTQK, in which Gln481Lys is essential to its lactate polymerizing activity. Among 19 A510X mutants, 15 synthesize lactate-3-hydroxybutanoate copolymers
A81E
-
in vitro activity is 108% of wild-type activity
A81G
-
in vitro activity is 99% of wild-type activity
A81M
-
in vitro activity is 101% of wild-type activity
A81P
-
in vitro activity is 105% of wild-type activity
C319A
C438G
-
no detectable activity
D281_D290del
-
no detectable activity
D480N
-
0.004% of the wild-type activity
E267K
-
40% of wild-type activity
E578_A589del
-
no detectable activity
F396L
-
about 40% of the poly(3-hydroxybutyrate) content compared to wild-type
F420A
-
poly(3-hydroxybutyrate) content is about 20% of wild-type value
F420C
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
f420D
-
poly(3-hydroxybutyrate) content is about 20% of wild-type value
F420E
-
poly(3-hydroxybutyrate) content is about 10% of wild-type value
F420G
-
poly(3-hydroxybutyrate) content is about 20% of wild-type value
F420H
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
F420I
-
poly(3-hydroxybutyrate) content is about 30% of wild-type value
F420K
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
F420L
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
F420M
-
poly(3-hydroxybutyrate) content is about 40% of wild-type value
F420N
-
poly(3-hydroxybutyrate) content is about 45% of wild-type value
F420Q
-
poly(3-hydroxybutyrate) content is about 30% of wild-type value
F420R
-
poly(3-hydroxybutyrate) content is about 30% of wild-type value
F420S
-
F420S enzyme has a significant decrease in its lag phase compared to that of the wild-type enzyme. Poly(3-hydroxybutyrate) content is about 85% of wild-type value
F420T
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
F420V
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
F420W
-
poly(3-hydroxybutyrate) content is about 25% of wild-type value
F420Y
-
poly(3-hydroxybutyrate) content is about 35% of wild-type value
G4A
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 14% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4C
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 24% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4D
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4D/F420S
-
mutant shows a higher poly(3-hydroxybutyrate) content and in vivo concentration of PhaCRe enzyme than the F420S mutant, the molecular weight of the poly(3-hydroxybutyrate) polymer of the double mutant is similar to that of the F420S mutant
G4E
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4F
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 45% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4H
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4I
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4K
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4L
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 2% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4M
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 24% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4N
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 57% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4P
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4Q
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 55% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4R
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4S
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4T
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4V
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 12% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4W
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 13% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4Y
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
H481Q
-
20% of the wild-type activity
H508Q
-
less than 0.0005% of the wild-type activity
L446K
-
15% of wild-type activity, no change in substrate specificity
N208D
-
about 40% of the poly(3-hydroxybutyrate) content compared to wild-type
T231I
-
no detectable activity
T323S
-
no detectable activity
V585_A589del
-
no detectable activity
Y445F
-
38% of wild-type activity, no change in substrate specificity
Y75E
-
in vitro activity is 137% of wild-type activity
Y75E/A81E
-
in vitro activity is 154% of wild-type activity
Y75F
-
in vitro activity is 104% of wild-type activity
Y75F/A81M
-
in vitro activity is 105% of wild-type activity
Y75G
-
in vitro activity is 110% of wild-type activity
Y75G/A81G
-
in vitro activity is 119% of wild-type activity
Y75P
-
in vitro activity is 138% of wild-type activity
Y75P/A81P
-
in vitro activity is 162% of wild-type activity
A510S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutant is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
-
A510X
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutation corresponds to position 481 in the class II lactate polymerizing polyhydroxyalkanoate synthase PhaC1PsSTQK, in which Gln481Lys is essential to its lactate polymerizing activity. Among 19 A510X mutants, 15 synthesize lactate-3-hydroxybutanoate copolymers
-
C319A
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
site-directed mutagenesis
-
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
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
Q482K
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
S326T
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
S326T/Q482K
site-directed mutagenesis, the double mutant grown on nonanoic acid in Pseudomonas putida strain GPp104 or grown on valeric acid in Ralstonia eutropha strain PHB-4 shows a 2.5fold higher copolymer content with 3.8fold increased 3-hydroxyalkanoate fraction compared to wild-type
Q482K
-
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
-
S326T
-
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
-
S326T/Q482K
-
site-directed mutagenesis, the double mutant grown on nonanoic acid in Pseudomonas putida strain GPp104 or grown on valeric acid in Ralstonia eutropha strain PHB-4 shows a 2.5fold higher copolymer content with 3.8fold increased 3-hydroxyalkanoate fraction compared to wild-type
-
E130D/S325T/S477G/Q481K
A547V
-
mutation increases polyhydroxyalkanoate yields
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
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
L484V
-
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
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
S482G
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
A547V
-
mutation increases polyhydroxyalkanoate yields
-
L484V
-
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
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
S482G
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
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
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
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
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
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
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E115K/S325C
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
E130D
-
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
-
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
-
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
-
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
-
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
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
L20P/Q481R
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
N16T/M292V/S325T
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
N5D/Q481K
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
Q481K
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
Q481M
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
Q481R
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
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
S325C
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
S325C/H350T
-
highly enhanced synthesis of poly(3-hydroxybutyrate)
S325T
S325T/Q481K
-
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
-
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
-
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
-
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/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 27 wt %) and an alteration of substrate specificity
Q481K
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
Q481M
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
Q481R
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
S325C
the mutation causes a significant increase in the incorporation of short-chain-length (SCL) in the PHA synthesized
S325C/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 21 wt %) and an alteration of substrate specificity
S325T
the mutation causes a significant increase in the incorporation of short-chain-length (SCL) in the PHA synthesized
S325T/Q481K
the mutat shows significantly increased incorporation of short-chain-length (SCL) substrates in the polymer synthesized by class II PhaCs
S325T/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 17 wt %) and an alteration of substrate specificity
S477A
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477F
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477G
S477H
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477R
S477R/Q481K
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 1 wt %) and an alteration of substrate specificity
S477R/Q481M
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 6 wt %) and an alteration of substrate specificity
S477R/Q481R
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 0.2 wt %) and an alteration of substrate specificity
S477Y
-
the mutation results in a shift in substrate specificity to smaller monomer units
E130D/S325T/S477G/Q481K
-
engineered polyhydroxybutanoate synthase able to accept 2-hydroxyacyl-CoAs as substrates
-
S324T/Q480K
-
the mutant shows increased activity compared to the wild type enzyme
S326T/Q482K
additional information