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(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxy-4-methylvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyalkanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyalkanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
(3R)-3-hydroxybutyryl-CoA + poly[5-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-5-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
(3R)-3-hydroxyvaleryl-CoA + poly[(R)-3-hydroxyvalerate]n
CoA + poly[(R)-3-hydroxyvalerate]n+1
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
(R)-3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
(R)-lactoyl-CoA + (3R)-3-hydroxybutyryl-CoA
CoA + poly(lactate-co-3-hydroxybutyrate)
-
-
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
3-hydroxybutyryl-CoA + 3-hydroxyhexanoate
poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
3-hydroxybutyryl-CoA + 3-hydroxyvaleryl-CoA
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
mutant enzymes
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[3-hydroxybutyrate](n+1) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
3-hydroxypropanoyl-CoA + (3-hydroxypropanoate)n
[(R)-3-hydroxypropanoate](n+1) + CoA
-
the value of the number-average molecular weight of the polymer obtained at a molar ratio of monomer-to-enzyme of 5000 is 25000 while the polydispersity is 4.7
-
-
?
3-hydroxypropanoyl-CoA + 3-hydroxybutanoyl-CoA
poly(3-hydroxypropanoate-co-3-hydroxybutanoate) + CoA
-
-
-
-
?
3-hydroxyvaleryl-CoA + [3-hydroxyvalerate]n
[3-hydroxyvalerate](n+1) + CoA
-
-
-
?
4-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[4-hydroxybutanoate](n+1) + CoA
-
-
-
?
DL-3-beta-hydroxybutyryl-CoA + poly[DL-3-hydroxybutyrate]n
CoA + poly[DL-3-hydroxybutyrate]n+1
-
-
-
-
?
DL-3-hydroxbutyryl-CoA + poly[DL-3-hydroxybutyrate]n
CoA + poly[DL-3-hydroxybutyrate]n+1
-
-
-
?
additional information
?
-
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
an inherent property of the synthase is chain termination and reinitiation. Class III PhaCPhaEAv synthase initiates polymerization through selfpriming. The primed synthase, species I, can serve as a substrate for further polyhydroxybutanoate elongation. Since hydroxybutyryl units can be added onto the existing polymers when HB-CoA is introduced into a reaction mixture containing preformed intermediate species, the reaction catalyzed by PhaCPhaEAv is nonprocessive. When enough (R)-3-hydroxybutyryl-CoA (S/E ratio is high) is available to load all of the enzyme present, the polymerization may be processive such that no intermediates can be detected and preformed oligomers cannot be extended
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
rate of elongation is much faster than the rate of initiation. The protein is uniformly loaded by a a single CoA/PhaC. Priming with the artificial primer sTCoA, i.e. a trimer of (R)-3-hydroxybutyryl-CoA in which the terminal OH group is replaced with a 3H, increases the uniformity of elongation, allowing distinct polymerization species to be observed. In the absence of (R)-3-hydroxybutyryl-CoA, a dimer of (R)-3-hydroxybutyryl-CoA is formed with a rate constant of 0.017 per s. The dimer forms via attack of CoA on the oxoester of the trimer of (R)-3-hydroxybutyryl-CoA-enzyme chain, leaving the synthase attached to a single (R)-3-hydroxybutyryl unit
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
I3R9Z3; I3R9Z4
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
PHB synthase exhibits positive cooperativity
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
PHB synthase exhibits positive cooperativity
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HCCoA
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HCCoA
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HCCoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
activity is 43% of the reaction with 3-hydroxybutyryl-CoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
activity is 10% of the reaction with 3-hydroxybutyryl-CoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HVCoA
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HVCoA
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HVCoA
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HHxeCoA
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxeCoA, low activity
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxeCoA
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HHxyCoA
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxyCoA, low activity
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxyCoA
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HABCoA
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HABCoA, low activity
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HABCoA
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
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
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
the PhaC-(His)6 protein catalyzes polymerization with a specific activity of 0.9 unit/mg. The PhaE-(His)6 protein is inactive. Addition of PhaE-(His)6 to PhaC-(His)6 increases the activity several 100fold. PhaC contains all the elements essential for catalysis and the polymerization proceeds by covalent catalysis using C149 and potentially C130
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-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
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
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
Ralstonia eutropha synthase possesses an essential catalytic dyad (C319-H508) in which the C319 is involved in covalent catalysis. A conserved Asp, D480, is not required for acylation of C319 by sT-CoA and is proposed to function as a general base catalyst to activate the hydroxyl of HBCoA for ester formation
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
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3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
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3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
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3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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less than 2% of the activity with 3-hydroxybutyryl-CoA: (R)-3-hydroxyhexanoyl-CoA, 3-hydroxypropionyl-CoA, (2R,3R)-2-methyl-3-hydroxylbutyryl-CoA, (R)-3-hydroxybutyryl (D)-pantetheine thioester, (R)-lactyl-CoA
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additional information
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synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class I PHA synthases, overview. The HHxyCoA and HABCoA can be efficiently incorporated into the polymers produced by enzyme PhaECAv. HHxCoA can be metabolically generated from 3-(R)-hydroxy-5-hexynoic acid. The activity of PhaECAv drops significantly with increasing length of the side chain in substrates. For example, the polymerization rates of HVCoA, HHxCoA, and HCCoA catalyzed by PhaECAv are measured at 23%, 0.38%, and 0.005% rate of HBCoA, respectively. No or poor activity with 3-(R)-hydroxy-4-phenylbutyryl-CoA (HPBCoA). Class III PhaECAv can polymerize HABCoA 6.5fold faster than HHxyCoA
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additional information
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the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
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additional information
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the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
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additional information
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enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
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additional information
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enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
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additional information
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enzyme shows both PHA polymerization and alcoholysis activities. For alcoholysis, PhaRC utilizes various alcohols other than ethanol for alcoholysis, leading to the PHA carboxy terminus modified with thiol, alkynyl, hydroxy, and benzyl groups
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additional information
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the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
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additional information
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the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
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additional information
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enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
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additional information
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enzyme shows both PHA polymerization and alcoholysis activities. For alcoholysis, PhaRC utilizes various alcohols other than ethanol for alcoholysis, leading to the PHA carboxy terminus modified with thiol, alkynyl, hydroxy, and benzyl groups
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additional information
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the transformant Cupriavidus necator PHB-4 harbouring Burkholderia sp. enzyme gene accumulates poly(3-hydroxybutyrate-co-4-hydroxybutyrate) with 4-hydroxybutyrate monomer as high as up to 87 mol% from sodium 4-hydroxybutyrate. The wild type Burkholderia sp. does not have the ability to produce this copolymer
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additional information
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synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. PhaCCc displays 2.5fold lower activity with HABCoA than with HHxyCoA
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additional information
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synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. PhaCCc displays 2.5fold lower activity with HABCoA than with HHxyCoA
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. Priming of PhaCCc with saturated trimeric HBCoA (named sTCoA) demonstrates that approximately one equivalent CoA per PhaC is released during enzyme assay. This is quite different from other reported class I synthases. Wild-type PhaCCs has similar activities toward HHxyCoA and HABCoA
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additional information
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no or less than 1% of the activity with 3-hydroxybutyryl-CoA: (R)-3-hydroxyhexanoyl-CoA, 3-hydroxypropionyl-CoA, (S)-3-hydroxybutyryl-CoA, (2R,3R)-2-methyl-3-hydroxylbutyryl-CoA, (R)-3-hydroxybutyryl (D)-pantetheine thioester, 4-hydroxybutyryl-CoA, (R)-lactyl-CoA
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
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additional information
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the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
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additional information
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I3R9Z3; I3R9Z4
the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
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additional information
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the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
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additional information
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3-hydroxyvaleryl-CoA, 4-hydroxybutyryl-CoA, and 3-hydroxydecanoyl-CoA are not accepted as substrates
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additional information
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3-hydroxyvaleryl-CoA, 4-hydroxybutyryl-CoA, and 3-hydroxydecanoyl-CoA are not accepted as substrates
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additional information
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the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile atty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview
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additional information
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the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
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additional information
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the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
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additional information
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the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
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additional information
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the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
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additional information
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PHA biosynthesis and in vitro PhaC enzymatic assay results show that the uncharacterized putative PHA synthase from Janthinobacterium sp. UMAB-58 is not funtional
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additional information
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PHA biosynthesis and in vitro PhaC enzymatic assay results show that the uncharacterized putative PHA synthase from Janthinobacterium sp. UMAB-60 is funtional
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additional information
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Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
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additional information
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analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
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additional information
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analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
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additional information
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analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
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additional information
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analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
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additional information
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analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
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additional information
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analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
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additional information
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analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
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additional information
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analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
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additional information
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Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
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additional information
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Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
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additional information
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Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
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additional information
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the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
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additional information
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structure-function relationship of PhaCs, and substrate specificity, overview
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additional information
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Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
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additional information
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no activity with (R)-3-hydroxypropionate and (R)-3-hydroxyvalerate
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additional information
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recombinant enzyme, expressed in phaC-deficient Cupriavidus necator, is able to accumulate PHA homopolymers and copolymers including poly(3-hydroxybutyrate) [P(3HB)], poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [P(3HB-co-3HV)], poly(3-hydroxybutyrate-co-5-hydroxyvalerate) [P(3HB-co-5HV)], poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)], poly(3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate) [P(3HB-co-3H4MV)], and poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(3HB-co-3HHx)], when suitable precursors are provided
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additional information
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the polyhydroxyalkanoate (PHA) synthase (PhaC) from a mangrove soil metagenome possesses a very wide substrate specificity. The enzyme shows the ability to incorporate six types of PHA monomers, 3-hydroxybutyrate (3HB), 3-hydroxyvalerate (3HV), 4-hydroxybutyrate (4HB), 3-hydroxy-4-methylvalerate (3H4MV), 5-hydroxyvalerate (5HV) and 3-hydroxyhexanoate (3HHx) in the presence of suitable precursors
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