Difference between revisions of "Part:BBa K1065000"
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<partinfo>BBa_K1065000 short</partinfo>
 
<partinfo>BBa_K1065000 short</partinfo>
  
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<html>2-oxoglutarate oxygenase/decarboxylase is an Ethylene Forming Enzyme (EFE) that catalyze Ethylene biosynthesis from 2-oxoglutarate. This enzyme was firstly purified  from <I>Pseudomonas Siringae</I> pv. <I>phaseolicola</I> PK2, a 2-oxoglutarate-dependent ethylene producing bacterium. The CDS has been optimized for both <I>E.coli</I> and <I>B.subtilis</i>.
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<html>2-oxoglutarate oxygenase/decarboxylase is an Ethylene Forming Enzyme (EFE) that catalyze Ethylene biosynthesis from 2-oxoglutarate. This enzyme was firstly purified  from <I>Pseudomonas Siringae</I> pv. <I>phaseolicola</I> PK2, a 2-oxoglutarate-dependent ethylene producing bacterium <a href="#ref1" id="ret_ref1">[1]</a>. The CDS has been optimized for both <I>E.coli</I> and <I>B.subtilis</i>.
 
</html>
 
</html>
  
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===Usage and Biology===
 
===Usage and Biology===
  
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The enzyme was studied deeply by many reasearch groups. It was purified and characterized with an <i>in vitro</i> test <a href="#ref2" id="ret_ref2">[2]</a>. It was then transformed and ectopically express in <i>E.coli</i> <a href="#ref3" id="ret_ref3">[3]</a> and in <i>Synecocystis sp</i> <a href="#ref4" id="ret_ref4">[4]</a>.
  
 
<hr>
 
<hr>
 
<ol><li>GOTO,M .,I SHIDAY, .,T AKIKAWAY,. & HYODOH,. (1985). Ethylene
 
<ol><li>GOTO,M .,I SHIDAY, .,T AKIKAWAY,. & HYODOH,. (1985). Ethylene
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production by the Kudzu strains of <I>Pseudomonas syringae</I> pv. <I>phaseolicola</I> causing halo blight in Pueraria lobata (Willd) Ohwi. Plant and Cell Physiology 26, 141-150.</li>
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production by the Kudzu strains of <I>Pseudomonas syringae</I> pv. <I>phaseolicola</I> causing halo blight in Pueraria lobata (Willd) Ohwi. Plant and Cell Physiology 26, 141-150. </li><a href="#ret_ref1" id="ref1">Return</a>
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<li>Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, et al. (1991) Purification and properties of an ethylene-forming enzyme from <I>Pseudomonas syringae </I>pv.<I> phaseolicola</I> PK2. Journal of General Microbiology 137: 2281–2286.</li>
+
<li>Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, et al. (1991) Purification and properties of an ethylene-forming enzyme from <I>Pseudomonas syringae </I>pv.<I> phaseolicola</I> PK2. Journal of General Microbiology 137: 2281–2286.</li> </li><a href="#ret_ref2" id="ref2">Return</a>
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<li>Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, et al. (1992) Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of <I>Pseudomonas syringae </I>pv.<I> phaseolicola</I> PK2. Biochem Biophys Res Commun 188: 826–832.</li>
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<li>Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, et al. (1992) Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of <I>Pseudomonas syringae </I>pv.<I> phaseolicola</I> PK2. Biochem Biophys Res Commun 188: 826–832.</li> </li><a href="#ret_ref3" id="ref3">Return</a>
 
<li>Fernando Guerrero, Vero´ nica Carbonell., Matteo Cossu., Danilo Correddu, Patrik R. Jones (2012) Ethylene Synthesis and Regulated Expression of
 
<li>Fernando Guerrero, Vero´ nica Carbonell., Matteo Cossu., Danilo Correddu, Patrik R. Jones (2012) Ethylene Synthesis and Regulated Expression of
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Recombinant Protein in <I>Synechocystis sp.</I> PCC 6803. PLoS ONE 7(11): e50470.</li></ol>
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Recombinant Protein in <I>Synechocystis sp.</I> PCC 6803. PLoS ONE 7(11): e50470.</li></li><a href="#ret_ref4" id="ref4">Return</a></ol>
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 09:47, 25 June 2013

2-oxoglutarate oxygenase/decarboxylase (EFE)

2-oxoglutarate oxygenase/decarboxylase is an Ethylene Forming Enzyme (EFE) that catalyze Ethylene biosynthesis from 2-oxoglutarate. This enzyme was firstly purified from Pseudomonas Siringae pv. phaseolicola PK2, a 2-oxoglutarate-dependent ethylene producing bacterium [1]. The CDS has been optimized for both E.coli and B.subtilis.

Usage and Biology

The enzyme was studied deeply by many reasearch groups. It was purified and characterized with an in vitro test <a href="#ref2" id="ret_ref2">[2]</a>. It was then transformed and ectopically express in E.coli <a href="#ref3" id="ret_ref3">[3]</a> and in Synecocystis sp <a href="#ref4" id="ret_ref4">[4]</a>.

  1. GOTO,M .,I SHIDAY, .,T AKIKAWAY,. & HYODOH,. (1985). Ethylene production by the Kudzu strains of Pseudomonas syringae pv. phaseolicola causing halo blight in Pueraria lobata (Willd) Ohwi. Plant and Cell Physiology 26, 141-150.
    2. <a href="#ret_ref1" id="ref1">Return</a>
  2. Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, et al. (1991) Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. Journal of General Microbiology 137: 2281–2286.
    3. <a href="#ret_ref2" id="ref2">Return</a>
  3. Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, et al. (1992) Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem Biophys Res Commun 188: 826–832.
    4. <a href="#ret_ref3" id="ref3">Return</a>
  4. Fernando Guerrero, Vero´ nica Carbonell., Matteo Cossu., Danilo Correddu, Patrik R. Jones (2012) Ethylene Synthesis and Regulated Expression of Recombinant Protein in Synechocystis sp. PCC 6803. PLoS ONE 7(11): e50470.
    5. <a href="#ret_ref4" id="ref4">Return</a>

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 319
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 17
    Illegal AgeI site found at 1070
  • 1000
    COMPATIBLE WITH RFC[1000]