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evolution
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28 strains belonging to 15 genera in the family Halobacteriaceae, sequence comparisons, phylogenetic analysis, and analyses of conserved regions of type III PHA synthases, overview
evolution
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PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
evolution
PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
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Pseudomonas isolates are found to carry PHA synthase genes which fall into two different PHA gene clusters, namely Class I and Class II, which are involved in the biosynthesis of short-chain-length-PHA (SCL-PHA) and medium-chain-length-PHA (MCL-PHA), respectively
evolution
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Pseudomonas isolates are found to carry PHA synthase genes which fall into two different PHA gene clusters, namely Class I and Class II, which are involved in the biosynthesis of short-chain-length-PHA (SCL-PHA) and medium-chain-length-PHA (MCL-PHA), respectively
evolution
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the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. No other gene involved in PHA synthesis is detected in close proximity to the uncharacterized putative PHA synthase gene in the Janthinobacterium isolates, therefore it falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Both of the antarctic Janthinobacterium isolates (UMAB-56 and UMAB-60) have a similar Class I PHA gene cluster as the Jantinobactarium spp. SCL-PHA producers
evolution
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the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. No other gene involved in PHA synthesis is detected in close proximity to the uncharacterized putative PHA synthase gene in the Janthinobacterium isolates, therefore it falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Both of the antarctic Janthinobacterium isolates (UMAB-56 and UMAB-60) have a similar Class I PHA gene cluster as the Jantinobactarium spp. SCL-PHA producers
evolution
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the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. The uncharacterized putative PHA synthase gene in the Janthinobacterium isolates falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Multiple sequence alignment shows that the uncharacterized putative PHA synthase gene contains all the highly conserved amino acid residues and the proposed catalytic triad of PHA synthase. Proposal of the uncharacterized PHA synthase as the new Class V PhaC
evolution
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the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. The uncharacterized putative PHA synthase gene in the Janthinobacterium isolates falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Multiple sequence alignment shows that the uncharacterized putative PHA synthase gene contains all the highly conserved amino acid residues and the proposed catalytic triad of PHA synthase. Proposal of the uncharacterized PHA synthase as the new Class V PhaC
evolution
A0A1E8EW93; A0A1E8EW64
the three genes phaJ (CLAOCE_21160) and phaEC (CLAOCE_21150 and CLAOCE_21140) are clustered in Clostridium acetireducens and encode a (R)-enoyl-CoA hydratase as well as a type III PHA synthase. The genes phaJ and phaEC from Clostridium acetireducens share high sequence similarity compared to genes encoding enzymes involved in PHB formation such as phaJ from Rhodospirillum rubrum or Haloferax mediterranei (Rru_A2964, HFX_1483) and phaEC from Synechocystis sp. PCC 6803
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHA-SCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHA-MCL which contains 6-14 carbons in the monomer unit
evolution
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there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
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there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
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evolution
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there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
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evolution
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the three genes phaJ (CLAOCE_21160) and phaEC (CLAOCE_21150 and CLAOCE_21140) are clustered in Clostridium acetireducens and encode a (R)-enoyl-CoA hydratase as well as a type III PHA synthase. The genes phaJ and phaEC from Clostridium acetireducens share high sequence similarity compared to genes encoding enzymes involved in PHB formation such as phaJ from Rhodospirillum rubrum or Haloferax mediterranei (Rru_A2964, HFX_1483) and phaEC from Synechocystis sp. PCC 6803
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evolution
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there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
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evolution
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PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
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malfunction
mutation of residues S320, F333, S475, A479, Y492, and L506 affects the positioning of the catalytic triad residues, while mutation of F387 affects the enzyme's dimerization
malfunction
mutation of residues S325, F338, S477, Q481, Y494, and Q508 affects the positioning of the catalytic triad residues, while mutation of F392 affects the enzyme's dimerization
malfunction
mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
malfunction
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mutation of residues T349, F362, S501, A505, F518, and L532 affects the positioning of the catalytic triad residues, while mutation of F416 affects the enzyme's dimerization
malfunction
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mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
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malfunction
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mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
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malfunction
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mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
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metabolism
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PhaC is involved in the biosynthetic pathway for generation of (R)-3-hydroxybutyrate monomers from two acetyl-CoA molecules, and further of short-chain length polyhydroxyalkanoates, PHAs. The malonyl-CoA availability is a limiting factor to synthesis of poly(3-hydroxybutyrate), P(3HB), thus acetoacetyl-CoA synthetase, which is controlling the malonyl-CoA pool, is an important enzyme for increasing the P(3HB) production
metabolism
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
metabolism
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
metabolism
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PHA synthase is the critical enzyme in PHA biosynthesis
metabolism
PHA synthase is the critical enzyme in PHA biosynthesis
metabolism
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polyhydroxyalkanoate synthase is not the rate limiting enzyme of polyhydroxyalkanoate biosynthesis in Synechocystis sp. PCC6803
metabolism
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Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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metabolism
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Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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metabolism
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Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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metabolism
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Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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metabolism
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PHA synthase is the critical enzyme in PHA biosynthesis
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physiological function
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class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
physiological function
P(3HB) synthase catalyzes polymerization of the 3-hydroxybutyryl-CoA monomers, Pseudomonas sp. USM 4-55 is a soil isolated bacterium that possesses the ability to produce polyhydroxyalkanoates consisting of both poly(3-hydroxybutyrate) homopolymer and medium-chain length monomers (6 to 14 carbon atoms) when sugars or fatty acids are utilized as the sole carbon source
physiological function
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PHA accumulation rates in the differnt strains harboring type III PHA synthases, overview
physiological function
enzyme is able to produce poly(3-hydroxybutyrate) in recombinant Cupriavidus necator PHB-negative mutant under the control of the phaC1 promoter from Cupriavidus necator H16
physiological function
gene expression in a Cupriavidus necator polyhydroxyalkanoate-negative mutant results in the accumulation of significant amount of polyhydroxyalkanoate
physiological function
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heterologous expression of foreign PHA synthases in the single mutant lacking isoform PhaC2 and in a double mutant lacking both isoforms PhaC1 and PhaC2 results in a significant accumulation of polyhydroxybutanoate in all generated strains. Six of the thirteen generated phaC hybrid vectors lead to an increased polyhydroxybutanoate accumulation in the single mutant in comparison to the wild type strain. All recombinant strains of Rthe double mutant harboring heterologous phaC genes accumulate significantly less polyhydroxybutanoate than the recombinant single mutants and the wild type strain. Recombinant strains with higher content of accumulated polyhydroxybutanoate are linked to higher growth rates and higher maximum ODs, due to the light scattering effect of polyhydroxybutanoate granules. All recombinant strains of the double mutant show significantly decreased growth rates and maximum ODs
physiological function
recombinant Escherichia coli expressing PHA synthase from Bacillus cereus shows a reduction of the molecular weight of PHA produced during the stationary phase of growth. Its carboxy end structure is capped by ethanol, as the result of alcoholytic cleavage of PHA chains by PhaRC induced by endogenous ethanol. This scission reaction is also induced by exogenous ethanol in both in vivo and in vitro assays. In addition, PhaRC has alcoholysis activity for PHA chains synthesized by other synthases
physiological function
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Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA)
physiological function
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Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA)
physiological function
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Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA). The ability of UMAB-40 to produce SCL-MCL-PHA copolymers is likely due to the presence of both Class I and II PHA synthases in its genome
physiological function
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Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA). The PHA produced by UMAB-60 is a homopolymer containing C4 repeating units
physiological function
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Class II PHA synthases are involved in the biosynthesis of medium-chain-length-polyhydroxyalkanoates (MCL-PHA). Pseudomonas sp. UMAB-08 PHA gene cluster is very well conserved among the MCL-PHA producers
physiological function
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Class II PHA synthases are involved in the biosynthesis of medium-chain-length-polyhydroxyalkanoates (MCL-PHA). Pseudomonas sp. UMAB-08 PHA gene cluster is very well conserved among the MCL-PHA producers. Although UMAB-40 does not produce any homopolymer (PHA having only one type of monomeric unit), small peaks of the C4 position [3-hydroxybutyrate (3HB) monomer] in addition to larger peaks at C6 to C14 are detected. The ability of UMAB-40 to produce SCL-MCL-PHA copolymers is likely due to the presence of both Class I and II PHA synthases in its genome
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
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different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group
physiological function
different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group
physiological function
different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group. Specifically, the specific activity of PhaCCs toward propynyl analogue (HHxyCoA) is only 5fold less than that toward the classical substrate HBCoA
physiological function
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PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs). Structure comparisons and structure-function relationship of PhaCs, overview
physiological function
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PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
physiological function
PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
physiological function
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PhaC can polymerize high molecular weight hydrophobic PHA chains in the hydrophilic environment of the cell cytoplasm
physiological function
poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
physiological function
A0A1E8EW93; A0A1E8EW64
species that do contain type III PHA synthases (phaEC) are able to produce butyrate and possess in addition an (R)-enoyl-CoA hydratase (phaJ), suggesting that (R)-3-hydroxybutyryl-CoA is the starting point for PHB synthesis, whereas the (S)-isomer is used for butyrate formation
physiological function
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recombinant Escherichia coli expressing PHA synthase from Bacillus cereus shows a reduction of the molecular weight of PHA produced during the stationary phase of growth. Its carboxy end structure is capped by ethanol, as the result of alcoholytic cleavage of PHA chains by PhaRC induced by endogenous ethanol. This scission reaction is also induced by exogenous ethanol in both in vivo and in vitro assays. In addition, PhaRC has alcoholysis activity for PHA chains synthesized by other synthases
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physiological function
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PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
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physiological function
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PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
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physiological function
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enzyme is able to produce poly(3-hydroxybutyrate) in recombinant Cupriavidus necator PHB-negative mutant under the control of the phaC1 promoter from Cupriavidus necator H16
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physiological function
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poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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physiological function
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gene expression in a Cupriavidus necator polyhydroxyalkanoate-negative mutant results in the accumulation of significant amount of polyhydroxyalkanoate
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physiological function
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species that do contain type III PHA synthases (phaEC) are able to produce butyrate and possess in addition an (R)-enoyl-CoA hydratase (phaJ), suggesting that (R)-3-hydroxybutyryl-CoA is the starting point for PHB synthesis, whereas the (S)-isomer is used for butyrate formation
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physiological function
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PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
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physiological function
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class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
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physiological function
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poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
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physiological function
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P(3HB) synthase catalyzes polymerization of the 3-hydroxybutyryl-CoA monomers, Pseudomonas sp. USM 4-55 is a soil isolated bacterium that possesses the ability to produce polyhydroxyalkanoates consisting of both poly(3-hydroxybutyrate) homopolymer and medium-chain length monomers (6 to 14 carbon atoms) when sugars or fatty acids are utilized as the sole carbon source
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physiological function
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PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
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additional information
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comparison of P(3HB) biosynthesis by recombinant Cupriavidus necator PHB-4 harboring the synthase gene of Cupriavidus sp. USMAA2-4 from various plant oils
additional information
in the class II PhaC1 from Pseudomonas sp. 61-3 (PhaC1Ps), Ser325 stabilizes the catalytic cysteine through hydrogen bonding. Another residue, Gln508 of PhaC1Ps is located in a conserved hydrophobic pocket which is next to the catalytic Asp and His. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
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residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the Balpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. Closed form PhaCCs-CAT blocks the substrates from entering the catalytic pocket by covering the active site within the CAP subdomain, in particular, a short stretch of highly dynamic amino acids named LID region. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
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structure comparisons and structure-function relationship of PhaCs, overview. Phe362 and Phe518 of PhaC from Aeromonas caviae (PhaCAc) are assisting the dimer formation and maintaining the integrity of the core beta-sheet, respectively. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
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residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
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additional information
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residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
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additional information
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residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
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additional information
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comparison of P(3HB) biosynthesis by recombinant Cupriavidus necator PHB-4 harboring the synthase gene of Cupriavidus sp. USMAA2-4 from various plant oils
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