Difference between revisions of "Part:BBa K3165002"

 
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Heme Oxygenase (ho1) is an enzyme that oxidises the heme group to biliverdin IX Alpha with the help of a ferredoxin cofactor. It catalyses the former of the two-step reaction involved in the biosynthesis of phycocyanobilins (PCBs).
 
Heme Oxygenase (ho1) is an enzyme that oxidises the heme group to biliverdin IX Alpha with the help of a ferredoxin cofactor. It catalyses the former of the two-step reaction involved in the biosynthesis of phycocyanobilins (PCBs).
  
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===Usage and Biology===
 
  
 
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'><b>Sequence and Features</b></span>
 
<partinfo>BBa_K3165002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3165002 SequenceAndFeatures</partinfo>
  
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===Usage and Biology===
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<h2> Biology </h2>
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Heme Oxygenase catalyzes the conversion of the Heme into Biliverdin IX Alpha with the use of a ferredoxin cofactor. It represents the first of the two steps involved in the biosynthesis of Phycocyanobilins (PCB). In association with phycocyanobilin ferredoxin reductase (PcyA) gene, the ho1 gene can stimulate the biosynthesis of phycocyanobilins.
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<h2> Usage </h2>
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This part can be used along with the PcyA gene (BBa_K3165003) to induce the production of phycocyanobilins. When incorporated into the CcaSR system and expressed in the <i>Escherichia coli</i>, we obtain the entire optogenetic system sensitive to green/red light in our bacteria.
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<h3> References : </h3>
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(1) https://www.uniprot.org/uniprot/P72849 <br>
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(2) Sugishima, M., Migita, C. T., Zhang, X., Yoshida, T., & Fukuyama, K. (2004). Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme. European Journal of Biochemistry, 271(22), 4517–4525. doi:10.1111/j.1432-1033.2004.04411.x <br>
  
 
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Revision as of 00:16, 18 October 2019


Heme Oxygenase (ho1) for Escherichia coli

Heme Oxygenase (ho1) is an enzyme that oxidises the heme group to biliverdin IX Alpha with the help of a ferredoxin cofactor. It catalyses the former of the two-step reaction involved in the biosynthesis of phycocyanobilins (PCBs).


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

Usage and Biology

Biology

Heme Oxygenase catalyzes the conversion of the Heme into Biliverdin IX Alpha with the use of a ferredoxin cofactor. It represents the first of the two steps involved in the biosynthesis of Phycocyanobilins (PCB). In association with phycocyanobilin ferredoxin reductase (PcyA) gene, the ho1 gene can stimulate the biosynthesis of phycocyanobilins.

Usage

This part can be used along with the PcyA gene (BBa_K3165003) to induce the production of phycocyanobilins. When incorporated into the CcaSR system and expressed in the Escherichia coli, we obtain the entire optogenetic system sensitive to green/red light in our bacteria.

References :

(1) https://www.uniprot.org/uniprot/P72849
(2) Sugishima, M., Migita, C. T., Zhang, X., Yoshida, T., & Fukuyama, K. (2004). Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme. European Journal of Biochemistry, 271(22), 4517–4525. doi:10.1111/j.1432-1033.2004.04411.x