Difference between revisions of "Part:BBa K801097:Design"

(Design Notes)
 
(4 intermediate revisions by 2 users not shown)
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<br>'''Keywords:'''
 
<br>'''Keywords:'''
<!--These keywords are necessary to find your part using a fulltext sarch.-->
+
Coumaryol-CoA, Coumaroyl-Coenzyme A, Xanthohumol, Biosynthesis, aromatic prenyltransferase
<!--keyword_1, keyword_2, keyword_3, keyword_4, keyword_5-->
+
  
 
<br>'''Abbreviations:'''
 
<br>'''Abbreviations:'''
<!--*used_abbreviation_1 = full_name_of_used_abbreviations_1-->
+
OMT = O-methyltransferase
<!--*used_abbreviation_2 = full_name_of_used_abbreviations_2-->
+
  
 
===Design Notes===
 
===Design Notes===
  
 
'''Related BioBrick:'''
 
'''Related BioBrick:'''
<!--*Other versions:[https://parts.igem.org/wiki/index.php?title=Part:BBa_?????? BBa_??????: Name_of_part] -->
+
 
<!--*Related BioBricks:[https://parts.igem.org/wiki/index.php?title=Part:BBa_?????? BBa_??????: Name_of_part]
+
Other versions: [https://parts.igem.org/Part:BBa_K801098 BBa_K801098: OMT1 coding region]
 +
 
 +
Related BioBricks:
 +
* [https://parts.igem.org/Part:BBa_K801090 BBa_K801090: phenylalanine ammonia lyase (PAL) + yeast consensus sequence]
 +
* [https://parts.igem.org/Part:BBa_K801091 BBa_K801091: phenylalanine ammonia lyase (PAL) coding region]
 +
* [https://parts.igem.org/Part:BBa_K801092 BBa_K801092: 4-coumarate - coenzym A ligase (4CL) + yeast consensus sequence]
 +
* [https://parts.igem.org/Part:BBa_K801093 BBa_K801093: 4-coumarate--coenzyme A ligase (4CL) coding region]
 +
* [https://parts.igem.org/Part:BBa_K801094 BBa_K801094: Naringenin - chalcone synthase (CHS) + yeast consensus sequence]
 +
* [https://parts.igem.org/Part:BBa_K801095 BBa_K801095: Naringenin - chalcone synthase (CHS) coding region]
 +
* [https://parts.igem.org/Part:BBa_K801096 BBa_K801096: Aromatic prenyltransferase (APT) coding region]
 +
* [https://parts.igem.org/Part:BBa_K801098 BBa_K801098: O-methyltransferase 1 (OMT1) coding region]
  
 
'''Cloning details:'''<br>
 
'''Cloning details:'''<br>
<!--*Designed in RFC10/RFC23/RFC25/RFC25_N-part-->
+
Designed in RFC10/RFC25
 
<!--*Mutation C889G to delete XbaI restriction site-->
 
<!--*Mutation C889G to delete XbaI restriction site-->
 
<!--*Truncation upstream/downstream compared to template, ?explanation?-->
 
<!--*Truncation upstream/downstream compared to template, ?explanation?-->
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<!--*Test digestion using ?enzyme1? & ?enzyme2?/Not yet performed-->
 
<!--*Test digestion using ?enzyme1? & ?enzyme2?/Not yet performed-->
 
<!--*Sequencing using primer ?primer_name?/Not yet sequenced-->
 
<!--*Sequencing using primer ?primer_name?/Not yet sequenced-->
<!--*Part was partly sequenced/Part was totally sequenced-->
+
Part was totally sequenced
  
 
'''Backbone:'''<br>
 
'''Backbone:'''<br>
<!--*Backbone name: pSB1C3'/?backbone_name?-->
+
*Backbone name: pSB1C3
<!--*Resistance: Amp/Cp/Kan/Tet-->
+
*Resistance: Cp
<!--*Copynumber: low/medium/high-->
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*Copynumber: high
  
 
'''Protein coding:'''<br>
 
'''Protein coding:'''<br>
<!--*Protein: ?Name_of_gene_product? [Nucleotide 1 to ???]-->
+
*Protein: O-methyltransferase
 
<!--*The protein has the amino acid replacements ???99??? to ???99???.-->
 
<!--*The protein has the amino acid replacements ???99??? to ???99???.-->
 
<!--*The protein encoded is posttranslationally modified by ???.-->
 
<!--*The protein encoded is posttranslationally modified by ???.-->
<!--*Tag: n-terminally fused/c-terminally fused His5/His6/Strep/Flag/other-->
+
*Tag: c-terminally fused Strep
  
'''Enzymatic activity:'''
+
'''Enzymatic activity:'''<br>
<!--none/EC-number ?.?.?.?-->
+
EC-number: EC 2.1.1
  
 
'''Cytotoxicity:'''<br>
 
'''Cytotoxicity:'''<br>
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'''Source:'''<br>
 
'''Source:'''<br>
 
<!--*Commercial system: plasmid name, system name, company name-->
 
<!--*Commercial system: plasmid name, system name, company name-->
<!--*Plasmid: p???, provided by ?name_of_person?, ?institute/university?, ?country?-->
+
Plasmid with OMT provided by Jonathan E. Page, National Research Council Canada, Plant Biotechnology Institute, Canada
 
<!--*Preexisting BioBrick ?Bba_number?-->
 
<!--*Preexisting BioBrick ?Bba_number?-->
 
<!--*cDNA Clone: ?clone_name?, ?company_name?-->
 
<!--*cDNA Clone: ?clone_name?, ?company_name?-->
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'''Organism:'''<br>
 
'''Organism:'''<br>
<!--*Genesequence derived from ''?organism_name?''-->
+
Genesequence derived from ''Humulus lupulus''
 
<!--*Codonoptimized for ''?organism_name?''-->
 
<!--*Codonoptimized for ''?organism_name?''-->
 
<!--*Designed for the following Chassis: ''?organism-name?''-->
 
<!--*Designed for the following Chassis: ''?organism-name?''-->
 
<!--*Statement about functionality in other chassis.-->
 
<!--*Statement about functionality in other chassis.-->
 
  
 
===References===
 
===References===
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'''Literature references:'''<br>
 
'''Literature references:'''<br>
<!--*[http://www.ncbi.nlm.nih.gov/pubmed/?PMID? '''Pubmed:''' ?Author(s)?, ?year?: ?title?]-->
+
[http://www.ncbi.nlm.nih.gov/pubmed/18223037 '''Pubmed''' : Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F., Page, J.E., 2008. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20, 186–200]
 +
 
  
 
'''Database references:'''<br>
 
'''Database references:'''<br>
<!--*[http://www.ncbi.nlm.nih.gov/nuccore/?accessNr? '''GenBank''': ?title?]-->
+
[http://www.ncbi.nlm.nih.gov/nuccore/EU309725.1 '''GenBank''': Humulus lupulus O-methyltransferase 1 (OMT1) mRNA, complete cds]
 +
 
 
<!--*[http://www.ebi.ac.uk/interpro/IEntry?ac=?accessNr? '''Interpro''': ?title?]-->
 
<!--*[http://www.ebi.ac.uk/interpro/IEntry?ac=?accessNr? '''Interpro''': ?title?]-->
<!--*[http://www.uniprot.org/uniprot/?accessNr? '''Uniprot''': ?title?]-->
+
[http://www.uniprot.org/uniprot/B0ZB55  '''Uniprot''': O-methyltransferase 1]
 
<!--*[http://pfam.sanger.ac.uk/family/?accessNr? '''Pfam:''' ?title?]-->
 
<!--*[http://pfam.sanger.ac.uk/family/?accessNr? '''Pfam:''' ?title?]-->
 
<!--*[http://www.rcsb.org/pdb/explore/explore.do?structureId=?accessNR? '''PDB:''' ?tile?]-->
 
<!--*[http://www.rcsb.org/pdb/explore/explore.do?structureId=?accessNR? '''PDB:''' ?tile?]-->
 
<!--*[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=?accessNr? '''Branda:''' ?title?]-->
 
<!--*[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=?accessNr? '''Branda:''' ?title?]-->

Latest revision as of 12:20, 3 October 2012

Chalcone O-methyltransferase (OMT1) + yeast consensus sequence


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 485
    Illegal XhoI site found at 300
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



http://www.ncbi.nlm.nih.gov/nucleotide/167613934/


Keywords: Coumaryol-CoA, Coumaroyl-Coenzyme A, Xanthohumol, Biosynthesis, aromatic prenyltransferase


Abbreviations: OMT = O-methyltransferase

Design Notes

Related BioBrick:

Other versions: BBa_K801098: OMT1 coding region

Related BioBricks:

Cloning details:
Designed in RFC10/RFC25

Quality control measures:
Part was totally sequenced

Backbone:

  • Backbone name: pSB1C3
  • Resistance: Cp
  • Copynumber: high

Protein coding:

  • Protein: O-methyltransferase
  • Tag: c-terminally fused Strep

Enzymatic activity:
EC-number: EC 2.1.1

Cytotoxicity:

Safety notes:

Intellectual property:

Corresponding part author/authors:

Source

Source:
Plasmid with OMT provided by Jonathan E. Page, National Research Council Canada, Plant Biotechnology Institute, Canada


Organism:
Genesequence derived from Humulus lupulus

References

Literature references:
[http://www.ncbi.nlm.nih.gov/pubmed/18223037 Pubmed : Nagel, J., Culley, L.K., Lu, Y., Liu, E., Matthews, P.D., Stevens, J.F., Page, J.E., 2008. EST analysis of hop glandular trichomes identifies an O-methyltransferase that catalyzes the biosynthesis of xanthohumol. Plant Cell 20, 186–200]


Database references:
[http://www.ncbi.nlm.nih.gov/nuccore/EU309725.1 GenBank: Humulus lupulus O-methyltransferase 1 (OMT1) mRNA, complete cds]

[http://www.uniprot.org/uniprot/B0ZB55 Uniprot: O-methyltransferase 1]