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Journal articles on the topic 'PHA synthases'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Hyakutake, Manami, Satoshi Tomizawa, Kouhei Mizuno, Hideki Abe, and Takeharu Tsuge. "Alcoholytic Cleavage of Polyhydroxyalkanoate Chains by Class IV Synthases Induced by Endogenous and Exogenous Ethanol." Applied and Environmental Microbiology 80, no. 4 (2013): 1421–29. http://dx.doi.org/10.1128/aem.03576-13.

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ABSTRACTPolyhydroxyalkanoate (PHA)-producingBacillusstrains express class IV PHA synthase, which is composed of the subunits PhaR and PhaC. RecombinantEscherichia coliexpressing PHA synthase fromBacillus cereusstrain YB-4 (PhaRCYB-4) showed an unusual reduction of the molecular weight of PHA produced during the stationary phase of growth. Nuclear magnetic resonance analysis of the low-molecular-weight PHA revealed that its carboxy end structure was capped by ethanol, suggesting that the molecular weight reduction was the result of alcoholytic cleavage of PHA chains by PhaRCYB-4induced by endog

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2

Alvarez-Santullano, Natalia, Pamela Villegas, Mario Sepúlveda Mardones, et al. "Genome-Wide Metabolic Reconstruction of the Synthesis of Polyhydroxyalkanoates from Sugars and Fatty Acids by Burkholderia Sensu Lato Species." Microorganisms 9, no. 6 (2021): 1290. http://dx.doi.org/10.3390/microorganisms9061290.

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Burkholderia sensu lato (s.l.) species have a versatile metabolism. The aims of this review are the genomic reconstruction of the metabolic pathways involved in the synthesis of polyhydroxyalkanoates (PHAs) by Burkholderia s.l. genera, and the characterization of the PHA synthases and the pha genes organization. The reports of the PHA synthesis from different substrates by Burkholderia s.l. strains were reviewed. Genome-guided metabolic reconstruction involving the conversion of sugars and fatty acids into PHAs by 37 Burkholderia s.l. species was performed. Sugars are metabolized via the Entne

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3

Chuah, Jo-Ann, Satoshi Tomizawa, Miwa Yamada, et al. "Characterization of Site-Specific Mutations in a Short-Chain-Length/Medium-Chain-Length Polyhydroxyalkanoate Synthase:In VivoandIn VitroStudies of Enzymatic Activity and Substrate Specificity." Applied and Environmental Microbiology 79, no. 12 (2013): 3813–21. http://dx.doi.org/10.1128/aem.00564-13.

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ABSTRACTSaturation point mutagenesis was carried out at position 479 in the polyhydroxyalkanoate (PHA) synthase fromChromobacteriumsp. strain USM2 (PhaCCs) with specificities for short-chain-length (SCL) [(R)-3-hydroxybutyrate (3HB) and (R)-3-hydroxyvalerate (3HV)] and medium-chain-length (MCL) [(R)-3-hydroxyhexanoate (3HHx)] monomers in an effort to enhance the specificity of the enzyme for 3HHx. A maximum 4-fold increase in 3HHx incorporation and a 1.6-fold increase in PHA biosynthesis, more than the wild-type synthase, was achieved using selected mutant synthases. These increases were subse

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4

Hall, Brian, Jennifer Baldwin, Ho Gun Rhie, and Douglas Dennis. "Cloning of the Nocardia corallina polyhydroxyalkanoate synthase gene and production of poly-(3-hydroxybutyrate-co-3-hydroxyhexanoate) and poly-(3-hydroxyvalerate-co-3-hydroxyheptanoate)." Canadian Journal of Microbiology 44, no. 7 (1998): 687–91. http://dx.doi.org/10.1139/w98-048.

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The polyhydroxyalkanoate (PHA) synthase gene (phaCNc) from Nocardia corallina was identified in a lambda library on a 6-kb BamHI fragment. A 2.8-kb XhoII subfragment was found to contain the ntact PHA synthase. This 2.8-kb fragment was subjected to DNA sequencing and was found to contain the coding region for the PHA synthase and a small downstream open reading frame of unknown function. On the basis of DNA sequence, phaCNc is closest in homology to the PHA synthases (phaCPaI and phaCPaII) of Pseudomonas aeruginosa (approximately 41% identity and 55% similarity). The 2.8-kb XhoII fragment cont

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5

Han, Jing, Jing Hou, Hailong Liu, et al. "Wide Distribution among Halophilic Archaea of a Novel Polyhydroxyalkanoate Synthase Subtype with Homology to Bacterial Type III Synthases." Applied and Environmental Microbiology 76, no. 23 (2010): 7811–19. http://dx.doi.org/10.1128/aem.01117-10.

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ABSTRACT Polyhydroxyalkanoates (PHAs) are accumulated as intracellular carbon and energy storage polymers by various bacteria and a few haloarchaea. In this study, 28 strains belonging to 15 genera in the family Halobacteriaceae were investigated with respect to their ability to synthesize PHAs and the types of their PHA synthases. Fermentation results showed that 18 strains from 12 genera could synthesize polyhydroxybutyrate (PHB) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV). For most of these haloarchaea, selected regions of the phaE and phaC genes encoding PHA synthases (type III)

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6

Kolibachuk, Dana, Andrea Miller, and Douglas Dennis. "Cloning, Molecular Analysis, and Expression of the Polyhydroxyalkanoic Acid Synthase (phaC) Gene fromChromobacterium violaceum." Applied and Environmental Microbiology 65, no. 8 (1999): 3561–65. http://dx.doi.org/10.1128/aem.65.8.3561-3565.1999.

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ABSTRACT The polyhydroxyalkanoic acid synthase gene fromChromobacterium violaceum (phaC Cv) was cloned and characterized. A 6.3-kb BamHI fragment was found to contain both phaC Cv and the polyhydroxyalkanoic acid (PHA)-specific 3-ketothiolase (phaA Cv). Escherichia coli strains harboring this fragment produced significant levels of PHA synthase and 3-ketothiolase, as judged by their activities. While C. violaceum accumulated poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) when grown on a fatty acid carbon source, Klebsiella aerogenes andRalstonia eutropha (formerly Alca

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7

Tsuge, Takeharu, Manami Hyakutake, and Kouhei Mizuno. "Class IV polyhydroxyalkanoate (PHA) synthases and PHA-producing Bacillus." Applied Microbiology and Biotechnology 99, no. 15 (2015): 6231–40. http://dx.doi.org/10.1007/s00253-015-6777-9.

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8

Martínez-Gutiérrez, Carolina A., Hever Latisnere-Barragán, José Q. García-Maldonado, and Alejandro López-Cortés. "Screening of polyhydroxyalkanoate-producing bacteria and PhaC-encoding genes in two hypersaline microbial mats from Guerrero Negro, Baja California Sur, Mexico." PeerJ 6 (May 7, 2018): e4780. http://dx.doi.org/10.7717/peerj.4780.

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Hypersaline microbial mats develop through seasonal and diel fluctuations, as well as under several physicochemical variables. Hence, resident microorganisms commonly employ strategies such as the synthesis of polyhydroxyalkanoates (PHAs) in order to resist changing and stressful conditions. However, the knowledge of bacterial PHA production in hypersaline microbial mats has been limited to date, particularly in regard to medium-chain length PHAs (mcl-PHAs), which have biotechnological applications due to their plastic properties. The aim of this study was to obtain evidence for PHA production

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9

Niamsiri, Nuttawee, Soazig C. Delamarre, Young-Rok Kim, and Carl A. Batt. "Engineering of Chimeric Class II Polyhydroxyalkanoate Synthases." Applied and Environmental Microbiology 70, no. 11 (2004): 6789–99. http://dx.doi.org/10.1128/aem.70.11.6789-6799.2004.

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ABSTRACT PHA synthase is a key enzyme involved in the biosynthesis of polyhydroxyalkanoates (PHAs). Using a combinatorial genetic strategy to create unique chimeric class II PHA synthases, we have obtained a number of novel chimeras which display improved catalytic properties. To engineer the chimeric PHA synthases, we constructed a synthetic phaC gene from Pseudomonas oleovorans (phaC1 Po ) that was devoid of an internal 540-bp fragment. Randomly amplified PCR products (created with primers based on conserved phaC sequences flanking the deleted internal fragment) were generated using genomic

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10

Hai, Tran, Daniela Lange, Ralf Rabus, and Alexander Steinbüchel. "Polyhydroxyalkanoate (PHA) Accumulation in Sulfate-Reducing Bacteria and Identification of a Class III PHA Synthase (PhaEC) in Desulfococcus multivorans." Applied and Environmental Microbiology 70, no. 8 (2004): 4440–48. http://dx.doi.org/10.1128/aem.70.8.4440-4448.2004.

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ABSTRACT Seven strains of sulfate-reducing bacteria (SRB) were tested for the accumulation of polyhydroxyalkanoates (PHAs). During growth with benzoate Desulfonema magnum accumulated large amounts of poly(3-hydroxybutyrate) [poly(3HB)]. Desulfosarcina variabilis (during growth with benzoate), Desulfobotulus sapovorans (during growth with caproate), and Desulfobacterium autotrophicum (during growth with caproate) accumulated poly(3HB) that accounted for 20 to 43% of cell dry matter. Desulfobotulus sapovorans and Desulfobacterium autotrophicum also synthesized copolyesters consisting of 3-hydrox

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11

AMARA, Amro A., and Bernd H. A. REHM. "Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: identification of catalytic residues." Biochemical Journal 374, no. 2 (2003): 413–21. http://dx.doi.org/10.1042/bj20030431.

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The class II PHA (polyhydroxyalkanoate) synthases [PHAMCL synthases (medium-chain-length PHA synthases)] are mainly found in pseudomonads and catalyse synthesis of PHAMCLs using CoA thioesters of medium-chain-length 3-hydroxyfatty acids (C6–C14) as a substrate. Only recently PHAMCL synthases from Pseudomonas oleovorans and Pseudomonas aeruginosa were purified and in vitro activity was achieved. A threading model of the P. aeruginosa PHAMCL synthase PhaC1 was developed based on the homology to the epoxide hydrolase (1ek1) from mouse which belongs to the α/β-hydrolase superfamily. The putative c

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12

Peters, Verena, and Bernd H. A. Rehm. "In Vivo Enzyme Immobilization by Use of Engineered Polyhydroxyalkanoate Synthase." Applied and Environmental Microbiology 72, no. 3 (2006): 1777–83. http://dx.doi.org/10.1128/aem.72.3.1777-1783.2006.

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ABSTRACT This study demonstrated that engineered polyhydroxyalkanoate (PHA) synthases can be employed as molecular tools to covalently immobilize enzymes at the PHA granule surface. The β-galactosidase was fused to the N terminus of the class II PHA synthase from Pseudomonas aeruginosa. The open reading frame was confirmed to encode the complete fusion protein by T7 promoter-dependent overexpression. Restoration of PHA biosynthesis in the PHA-negative mutant of P. aeruginosa PAO1 showed a PHA synthase function of the fusion protein. PHA granules were isolated and showed β-galactosidase activit

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13

REHM, Bernd H. A. "Polyester synthases: natural catalysts for plastics." Biochemical Journal 376, no. 1 (2003): 15–33. http://dx.doi.org/10.1042/bj20031254.

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Polyhydroxyalkanoates (PHAs) are biopolyesters composed of hydroxy fatty acids, which represent a complex class of storage polyesters. They are synthesized by a wide range of different Gram-positive and Gram-negative bacteria, as well as by some Archaea, and are deposited as insoluble cytoplasmic inclusions. Polyester synthases are the key enzymes of polyester biosynthesis and catalyse the conversion of (R)-hydroxyacyl-CoA thioesters to polyesters with the concomitant release of CoA. These soluble enzymes turn into amphipathic enzymes upon covalent catalysis of polyester-chain formation. A sel

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14

Matsusaki, Hiromi, Sumihide Manji, Kazunori Taguchi, Mikiya Kato, Toshiaki Fukui, and Yoshiharu Doi. "Cloning and Molecular Analysis of the Poly(3-hydroxybutyrate) and Poly(3-hydroxybutyrate-co-3-hydroxyalkanoate) Biosynthesis Genes in Pseudomonas sp. Strain 61-3." Journal of Bacteriology 180, no. 24 (1998): 6459–67. http://dx.doi.org/10.1128/jb.180.24.6459-6467.1998.

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ABSTRACT Two types of polyhydroxyalkanoate (PHA) biosynthesis gene loci (phb and pha) of Pseudomonas sp. strain 61-3, which produces a blend of poly(3-hydroxybutyrate) [P(3HB)] homopolymer and a random copolymer {poly(3-hydroxybutyrate-co-3-hydroxyalkanoate) [P(3HB-co-3HA]} consisting of 3HA units of 4 to 12 carbon atoms, were cloned and analyzed at the molecular level. In thephb locus, three open reading frames encoding polyhydroxybutyrate (PHB) synthase (PhbCPs), β-ketothiolase (PhbAPs), and NADPH-dependent acetoacetyl coenzyme A reductase (PhbBPs) were found. The genetic organization showed

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15

Mok, Pei-Shze, Jo-Ann Chuah, Nazalan Najimudin, Pauline-Woan-Ying Liew, Bor-Chyan Jong, and Kumar Sudesh. "In Vivo Characterization and Application of the PHA Synthase from Azotobacter vinelandii for the Biosynthesis of Polyhydroxyalkanoate Containing 4-Hydroxybutyrate." Polymers 13, no. 10 (2021): 1576. http://dx.doi.org/10.3390/polym13101576.

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Polyhydroxyalkanoate (PHA) is a biodegradable thermoplastic naturally synthesized by many microorganisms, and the PHA synthase (PhaC) is known to be the key enzyme involved in determining the material properties and monomer composition of the produced PHA. The ability to exploit widely distributed, commonly found soil microorganisms such as Azotobacter vinelandii to synthesize PHA containing the lipase-degradable 4-hydroxybutyrate (4HB) monomer will allow for convenient production of biocompatible and flexible PHA. Comparisons between the A. vinelandii wild type and mutant strains, with and wi

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16

Thomas, Tatiana, Kumar Sudesh, Alexis Bazire, et al. "PHA Production and PHA Synthases of the Halophilic Bacterium Halomonas sp. SF2003." Bioengineering 7, no. 1 (2020): 29. http://dx.doi.org/10.3390/bioengineering7010029.

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Among the different tools which can be studied and managed to tailor-make polyhydroxyalkanoates (PHAs) and enhance their production, bacterial strain and carbon substrates are essential. The assimilation of carbon sources is dependent on bacterial strain’s metabolism and consequently cannot be dissociated. Both must wisely be studied and well selected to ensure the highest production yield of PHAs. Halomonas sp. SF2003 is a marine bacterium already identified as a PHA-producing strain and especially of poly-3-hydroxybutyrate (P-3HB) and poly-3-hydroxybutyrate-co-3-hydroxyvalerate (P-3HB-co-3HV

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17

McCool, Gabriel J., and Maura C. Cannon. "PhaC and PhaR Are Required for Polyhydroxyalkanoic Acid Synthase Activity in Bacillus megaterium." Journal of Bacteriology 183, no. 14 (2001): 4235–43. http://dx.doi.org/10.1128/jb.183.14.4235-4243.2001.

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ABSTRACT Polyhydroxyalkanoic acids (PHAs) are a class of polyesters stored in inclusion bodies and found in many bacteria and in some archaea. The terminal step in the synthesis of PHA is catalyzed by PHA synthase. Genes encoding this enzyme have been cloned, and the primary sequence of the protein, PhaC, is deduced from the nucleotide sequences of more than 30 organisms. PHA synthases are grouped into three classes based on substrate range, molecular mass, and whether or not there is a requirement for phaE in addition to thephaC gene product. Here we report the results of an analysis of a PHA

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18

Peters, Verena, and Bernd H. A. Rehm. "In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases." FEMS Microbiology Letters 248, no. 1 (2005): 93–100. http://dx.doi.org/10.1016/j.femsle.2005.05.027.

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19

Mezzolla, Valeria, Oscar D’Urso, and Palmiro Poltronieri. "Role of PhaC Type I and Type II Enzymes during PHA Biosynthesis." Polymers 10, no. 8 (2018): 910. http://dx.doi.org/10.3390/polym10080910.

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PHA synthases (PhaC) are grouped into four classes based on the kinetics and mechanisms of reaction. The grouping of PhaC enzymes into four classes is dependent on substrate specificity, according to the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce scl-PHAs depending on propionate, butyrate, valerate and hexanoate precursors, while Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors. PHA synthases of Class I, in particular PhaCCs from Chromobacterium USM2 and PhaCCn/RePhaC1 from Cupriavidu

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20

Tariq, Aamira, Abdul Hameed, Habib Bokhari, and Farha Masood. "Is atomic rearrangement of type IV PHA synthases responsible for increased PHA production?" Journal of Biomolecular Structure and Dynamics 33, no. 6 (2014): 1225–38. http://dx.doi.org/10.1080/07391102.2014.941401.

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21

Rehm, Bernd H. A., and Alexander Steinbüchel. "Biochemical and genetic analysis of PHA synthases and other proteins required for PHA synthesis." International Journal of Biological Macromolecules 25, no. 1-3 (1999): 3–19. http://dx.doi.org/10.1016/s0141-8130(99)00010-0.

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22

HYAKUTAKE, Manami, Yuta SAITO, Satoshi TOMIZAWA, Kouhei MIZUNO, and Takeharu TSUGE. "Polyhydroxyalkanoate (PHA) Synthesis by Class IV PHA Synthases EmployingRalstonia eutrophaPHB−4 as Host Strain." Bioscience, Biotechnology, and Biochemistry 75, no. 8 (2011): 1615–17. http://dx.doi.org/10.1271/bbb.110229.

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23

Steinbüchel, Alexander, Kristin Aerts, Matthias Liebergesell, et al. "Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions." Canadian Journal of Microbiology 41, no. 13 (1995): 94–105. http://dx.doi.org/10.1139/m95-175.

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Some mathematical calculations were done that provided information about the structure and biochemistry of polyhydroxyalkanoic acid (PHA) granules and about the amounts of the different constituents that contribute to the PHA granules. The data obtained from these calculations are compared with data from the literature, which show that PHA granules consist not only of the polyester but also of phospholipids and proteins. The latter are referred to as granule-associated proteins, and they are always located at the surface of the PHA granules. A concept is proposed that distinguishes four classe

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24

A., Amara, Steinbüchel A., and Rehm B. "In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase: isolation and characterization of modified PHA synthases with enhanced activity." Applied Microbiology and Biotechnology 59, no. 4-5 (2002): 477–82. http://dx.doi.org/10.1007/s00253-002-1035-3.

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25

Tsuge, Takeharu, Kotaro Yano, Shin-ichi Imazu, et al. "Biosynthesis of Polyhydroxyalkanoate (PHA) Copolymer from Fructose Using Wild-Type and Laboratory-Evolved PHA Synthases." Macromolecular Bioscience 5, no. 2 (2005): 112–17. http://dx.doi.org/10.1002/mabi.200400152.

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26

Budde, Charles F., Sebastian L. Riedel, Laura B. Willis, ChoKyun Rha, and Anthony J. Sinskey. "Production of Poly(3-Hydroxybutyrate-co-3-Hydroxyhexanoate) from Plant Oil by Engineered Ralstonia eutropha Strains." Applied and Environmental Microbiology 77, no. 9 (2011): 2847–54. http://dx.doi.org/10.1128/aem.02429-10.

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ABSTRACTThe polyhydroxyalkanoate (PHA) copolymer poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(HB-co-HHx)] has been shown to have potential to serve as a commercial bioplastic. Synthesis of P(HB-co-HHx) from plant oil has been demonstrated with recombinantRalstonia eutrophastrains expressing heterologous PHA synthases capable of incorporating HB and HHx into the polymer. With these strains, however, short-chain-length fatty acids had to be included in the medium to generate PHA with high HHx content. Our group has engineered twoR. eutrophastrains that accumulate high levels of P(HB-co-HHx)

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27

Zhang, Wei, Chao Chen, Ruikai Cao, Leila Maurmann, and Ping Li. "Inhibitors of Polyhydroxyalkanoate (PHA) Synthases: Synthesis, Molecular Docking, and Implications." ChemBioChem 16, no. 1 (2014): 156–66. http://dx.doi.org/10.1002/cbic.201402380.

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28

Wang, Qian, Yongzhen Xia, Quan Chen, and Qingsheng Qi. "Incremental truncation of PHA synthases results in altered product specificity." Enzyme and Microbial Technology 50, no. 6-7 (2012): 293–97. http://dx.doi.org/10.1016/j.enzmictec.2012.02.003.

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29

Kouřilová, Xenie, Jana Schwarzerová, Iva Pernicová, et al. "The First Insight into Polyhydroxyalkanoates Accumulation in Multi-Extremophilic Rubrobacter xylanophilus and Rubrobacter spartanus." Microorganisms 9, no. 5 (2021): 909. http://dx.doi.org/10.3390/microorganisms9050909.

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Actinobacteria belonging to the genus Rubrobacter are known for their multi-extremophilic growth conditions—they are highly radiation-resistant, halotolerant, thermotolerant or even thermophilic. This work demonstrates that the members of the genus are capable of accumulating polyhydroxyalkanoates (PHA) since PHA-related genes are widely distributed among Rubrobacter spp. whose complete genome sequences are available in public databases. Interestingly, all Rubrobacter strains possess both class I and class III synthases (PhaC). We have experimentally investigated the PHA accumulation in two th

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30

Lu, Qiuhe, Jing Han, Ligang Zhou, Jian Zhou, and Hua Xiang. "Genetic and Biochemical Characterization of the Poly(3-Hydroxybutyrate-co-3-Hydroxyvalerate) Synthase in Haloferax mediterranei." Journal of Bacteriology 190, no. 12 (2008): 4173–80. http://dx.doi.org/10.1128/jb.00134-08.

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ABSTRACT The haloarchaeon Haloferax mediterranei has shown promise for the economical production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV), a desirable bioplastic. However, little is known at present about the genes involved in PHBV synthesis in the domain Archaea. In this study, we cloned the gene cluster (phaEC Hme) encoding a polyhydroxyalkanoate (PHA) synthase in H. mediterranei CGMCC 1.2087 via thermal asymmetric interlaced PCR. Western blotting revealed that the phaE Hme and phaC Hme genes were constitutively expressed, and both the PhaEHme and PhaCHme proteins were strongly

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Mezzina, Mariela P., and M. Julia Pettinari. "Phasins, Multifaceted Polyhydroxyalkanoate Granule-Associated Proteins." Applied and Environmental Microbiology 82, no. 17 (2016): 5060–67. http://dx.doi.org/10.1128/aem.01161-16.

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ABSTRACTPhasins are the major polyhydroxyalkanoate (PHA) granule-associated proteins. They promote bacterial growth and PHA synthesis and affect the number, size, and distribution of the granules. These proteins can be classified in 4 families with distinctive characteristics. Low-resolution structural studies andin silicopredictions were performed in order to elucidate the structure of different phasins. Most of these proteins share some common structural features, such as a preponderant α-helix composition, the presence of disordered regions that provide flexibility to the protein, and coile

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32

Umeda, Fusako, Tomohiro Nishikawa, Hitoshi Miyasaka, Isamu Maeda, Masaya Kawase, and Kiyohito Yagγ. "Short Communication: Homology Study of Two Polyhydroxyalkanoate (PHA) Synthases from Pseudomonas Aureofaciens." DNA Sequence 12, no. 4 (2001): 281–84. http://dx.doi.org/10.3109/10425170109025003.

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33

Clemente, T., D. Shah, M. Tran, et al. "Sequence of PHA synthase gene from two strains of Rhodospirillum rubrum and in vivo substrate specificity of four PHA synthases across two heterologous expression systems." Applied Microbiology and Biotechnology 53, no. 4 (2000): 420–29. http://dx.doi.org/10.1007/s002530051636.

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34

Zain, Noor-Afiqah Ahmad, Lee-Mei Ng, Choon Pin Foong, Yen Teng Tai, Jayaram Nanthini, and Kumar Sudesh. "Complete Genome Sequence of a Novel Polyhydroxyalkanoate (PHA) Producer, Jeongeupia sp. USM3 (JCM 19920) and Characterization of Its PHA Synthases." Current Microbiology 77, no. 3 (2020): 500–508. http://dx.doi.org/10.1007/s00284-019-01852-z.

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35

Xia, Yongzhen, Jan Hendrik Wübbeler, Qingsheng Qi, and Alexander Steinbüchel. "Employing a Recombinant Strain of Advenella mimigardefordensis for Biotechnical Production of Homopolythioesters from 3,3′-Dithiodipropionic Acid." Applied and Environmental Microbiology 78, no. 9 (2012): 3286–97. http://dx.doi.org/10.1128/aem.00007-12.

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ABSTRACTAdvenella mimigardefordensisstrain DPN7Twas genetically modified to produce poly(3-mercaptopropionic acid) (PMP) homopolymer by exploiting the recently unraveled process of 3,3′-dithiodipropionic acid (DTDP) catabolism. Production was achieved by systematically engineering the metabolism of this strain as follows: (i) deletion of its inherent 3MP dioxygenase-encoding gene (mdo), (ii) introduction of thebuk-ptboperon (genes encoding the butyrate kinase, Buk, and the phosphotransbutyrylase, Ptb, fromClostridium acetobutylicum), and (iii) overexpression of its own polyhydroxyalkanoate syn

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Solaiman, Daniel K. Y. "Biosynthesis of medium-chain-length poly(hydroxyalkanoates) with altered composition by mutant hybrid PHA synthases." Journal of Industrial Microbiology and Biotechnology 30, no. 5 (2003): 322–26. http://dx.doi.org/10.1007/s10295-003-0059-8.

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37

Hai, T., S. Hein, and A. Steinbüchel. "Multiple evidence for widespread and general occurrence of type-III PHA synthases in cyanobacteria and molecular characterization of the PHA synthases from two thermophilic cyanobacteria: Chlorogloeopsis fritschii PCC 6912 and Synechococcus sp. strain MA19." Microbiology 147, no. 11 (2001): 3047–60. http://dx.doi.org/10.1099/00221287-147-11-3047.

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Sato, Shun, Masayuki Minato, Yoshihiro Kikkawa, Hideki Abe, and Takeharu Tsuge. "In vitro synthesis of polyhydroxyalkanoate catalyzed by class II and III PHA synthases: a useful technique for surface coatings of a hydrophobic support with PHA." Journal of Chemical Technology & Biotechnology 85, no. 6 (2009): 779–82. http://dx.doi.org/10.1002/jctb.2261.

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Jia, Kaimin, Ruikai Cao, Duy H. Hua, and Ping Li. "Study of Class I and Class III Polyhydroxyalkanoate (PHA) Synthases with Substrates Containing a Modified Side Chain." Biomacromolecules 17, no. 4 (2016): 1477–85. http://dx.doi.org/10.1021/acs.biomac.6b00082.

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Matsumoto, Ken’ichiro, Kazuma Takase, Yoko Yamamoto, Yoshiharu Doi, and Seiichi Taguchi. "Chimeric Enzyme Composed of Polyhydroxyalkanoate (PHA) Synthases from Ralstonia eutropha and Aeromonas caviae Enhances Production of PHAs in Recombinant Escherichia coli." Biomacromolecules 10, no. 4 (2009): 682–85. http://dx.doi.org/10.1021/bm801386j.

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Yang, Taek Ho, Yu Kyung Jung, Hye Ok Kang, Tae Wan Kim, Si Jae Park, and Sang Yup Lee. "Tailor-made type II Pseudomonas PHA synthases and their use for the biosynthesis of polylactic acid and its copolymer in recombinant Escherichia coli." Applied Microbiology and Biotechnology 90, no. 2 (2011): 603–14. http://dx.doi.org/10.1007/s00253-010-3077-2.

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Sudesh, Kumar, Toshiaki Fukui, and Yoshiharu Doi. "Genetic Analysis of Comamonas acidovoransPolyhydroxyalkanoate Synthase and Factors Affecting the Incorporation of 4-Hydroxybutyrate Monomer." Applied and Environmental Microbiology 64, no. 9 (1998): 3437–43. http://dx.doi.org/10.1128/aem.64.9.3437-3443.1998.

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ABSTRACT The polyhydroxyalkanoate (PHA) synthase gene of Comamonas acidovorans DS-17 (phaCCa ) was cloned by using the synthase gene of Alcaligenes eutrophus as a heterologous hybridization probe. Complete sequencing of a 4.0-kbpSmaI-HindIII (SH40) subfragment revealed the presence of a 1,893-bp PHA synthase coding region which was followed by a 1,182-bp β-ketothiolase gene (phaACa ). Both the translated products of these genes showed significant identity, 51.1 and 74.2%, respectively, to the primary structures of the products of the corresponding genes in A. eutrophus. The arrangement of PHA

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Han, Jing, Qiuhe Lu, Ligang Zhou, Hailong Liu, and Hua Xiang. "Identification of the Polyhydroxyalkanoate (PHA)-Specific Acetoacetyl Coenzyme A Reductase among Multiple FabG Paralogs in Haloarcula hispanica and Reconstruction of the PHA Biosynthetic Pathway in Haloferax volcanii." Applied and Environmental Microbiology 75, no. 19 (2009): 6168–75. http://dx.doi.org/10.1128/aem.00938-09.

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ABSTRACT Genome-wide analysis has revealed abundant FabG (β-ketoacyl-ACP reductase) paralogs, with uncharacterized biological functions, in several halophilic archaea. In this study, we identified for the first time that the fabG1 gene, but not the other five fabG paralogs, encodes the polyhydroxyalkanoate (PHA)-specific acetoacetyl coenzyme A (acetoacetyl-CoA) reductase in Haloarcula hispanica. Although all of the paralogous fabG genes were actively transcribed, only disruption or knockout of fabG1 abolished PHA synthesis, and complementation of the ΔfabG1 mutant with the fabG1 gene restored

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Stubbe, JoAnne, and Jiamin Tian. "Polyhydroxyalkanoate (PHA) homeostasis: the role of the PHA synthase." Natural Product Reports 20, no. 5 (2003): 445. http://dx.doi.org/10.1039/b209687k.

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Ushimaru, K., Y. Motoda, K. Numata, and T. Tsuge. "Phasin Proteins Activate Aeromonas caviae Polyhydroxyalkanoate (PHA) Synthase but Not Ralstonia eutropha PHA Synthase." Applied and Environmental Microbiology 80, no. 9 (2014): 2867–73. http://dx.doi.org/10.1128/aem.04179-13.

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Chek, Min Fey, Ayaka Hiroe, Toshio Hakoshima, Kumar Sudesh, and Seiichi Taguchi. "PHA synthase (PhaC): interpreting the functions of bioplastic-producing enzyme from a structural perspective." Applied Microbiology and Biotechnology 103, no. 3 (2018): 1131–41. http://dx.doi.org/10.1007/s00253-018-9538-8.

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REHM, Bernd H. A., Qingsheng QI, Br Bernd BEERMANN, Hans-Jürgen HINZ, and Alexander STEINBÜCHEL. "Matrix-assisted in vitro refolding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli." Biochemical Journal 358, no. 1 (2001): 263–68. http://dx.doi.org/10.1042/bj3580263.

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In order to facilitate the large-scale preparation of active class II polyhydroxyalkanoate (PHA) synthase, we constructed a vector pT7-7 derivative that contains a modified phaC1 gene encoding a PHA synthase from Pseudomonas aeruginosa possessing six N-terminally fused histidine residues. Overexpression of this phaC1 gene under control of the strong Ø10 promoter was achieved in Escherichia coli BL21(DE3). The fusion protein was deposited as inactive inclusion bodies in recombinant E. coli, and contributed approx. 30% of total protein. The inclusion bodies were purified by selective solubilizat

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Hauf, Waldemar, Björn Watzer, Nora Roos, Alexander Klotz, and Karl Forchhammer. "Photoautotrophic Polyhydroxybutyrate Granule Formation Is Regulated by Cyanobacterial Phasin PhaP in Synechocystis sp. Strain PCC 6803." Applied and Environmental Microbiology 81, no. 13 (2015): 4411–22. http://dx.doi.org/10.1128/aem.00604-15.

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ABSTRACTCyanobacteria are photoautotrophic microorganisms which fix atmospheric carbon dioxide via the Calvin-Benson cycle to produce carbon backbones for primary metabolism. Fixed carbon can also be stored as intracellular glycogen, and in some cyanobacterial species likeSynechocystissp. strain PCC 6803, polyhydroxybutyrate (PHB) accumulates when major nutrients like phosphorus or nitrogen are absent. So far only three enzymes which participate in PHB metabolism have been identified in this organism, namely, PhaA, PhaB, and the heterodimeric PHB synthase PhaEC. In this work, we describe the c

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Park, Si Jae, and Sang Yup Lee. "Identification and Characterization of a New Enoyl Coenzyme A Hydratase Involved in Biosynthesis of Medium-Chain-Length Polyhydroxyalkanoates in Recombinant Escherichia coli." Journal of Bacteriology 185, no. 18 (2003): 5391–97. http://dx.doi.org/10.1128/jb.185.18.5391-5397.2003.

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ABSTRACT The biosynthetic pathway of medium-chain-length (MCL) polyhydroxyalkanoates (PHAs) from fatty acids has been established in fadB mutant Escherichia coli strain by expressing the MCL-PHA synthase gene. However, the enzymes that are responsible for the generation of (R)-3-hydroxyacyl coenzyme A (R3HA-CoAs), the substrates for PHA synthase, have not been thoroughly elucidated. Escherichia coli MaoC, which is homologous to Pseudomonas aeruginosa (R)-specific enoyl-CoA hydratase (PhaJ1), was identified and found to be important for PHA biosynthesis in a fadB mutant E. coli strain. When the

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Brockelbank, Jane A., Verena Peters, and Bernd H. A. Rehm. "Recombinant Escherichia coli Strain Produces a ZZ Domain Displaying Biopolyester Granules Suitable for Immunoglobulin G Purification." Applied and Environmental Microbiology 72, no. 11 (2006): 7394–97. http://dx.doi.org/10.1128/aem.01014-06.

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ABSTRACT The immunoglobulin G (IgG) binding ZZ domain of protein A from Staphylococcus aureus was fused to the N terminus of the polyhydroxyalkanoate (PHA) synthase from Cupriavidus necator. The fusion protein was confirmed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and mediated formation of ZZ domain-displaying PHA granules in recombinant Escherichia coli. The IgG binding capacity of isolated granules was assessed using enzyme-linked immunosorbent assay and could be enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient pu

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