Difference between revisions of "Part:BBa K801091:Design"
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PMID: 15932991 | PMID: 15932991 | ||
<br>'''Keywords:''' | <br>'''Keywords:''' | ||
− | + | Coumaryol-CoA, Coumaroyl-Coenzyme A, Xanthohumol, Biosynthesis, 4-coumarate-coenzyme A ligase | |
− | + | ||
<br>'''Abbreviations:''' | <br>'''Abbreviations:''' | ||
+ | PAL = Phenylalanine Ammonia Lyase | ||
<!--*used_abbreviation_1 = full_name_of_used_abbreviations_1--> | <!--*used_abbreviation_1 = full_name_of_used_abbreviations_1--> | ||
<!--*used_abbreviation_2 = full_name_of_used_abbreviations_2--> | <!--*used_abbreviation_2 = full_name_of_used_abbreviations_2--> | ||
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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 totally sequenced | |
'''Backbone:'''<br> | '''Backbone:'''<br> | ||
− | + | Backbone name: pSB1C3 | |
− | + | Resistance: Cp | |
<!--*Copynumber: low/medium/high--> | <!--*Copynumber: low/medium/high--> | ||
'''Protein coding:'''<br> | '''Protein coding:'''<br> | ||
− | + | Protein: Phenylalanine Ammonia Lyase | |
<!--*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 ???.--> | ||
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'''Enzymatic activity:''' | '''Enzymatic activity:''' | ||
− | + | EC-number 4.3.1.25 | |
'''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: pKS2µHyg-PAL-4CL-CHS, provided by John A. Morgan, Purdue University, USA | |
<!--*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 ''Rhodosporidium toruloides' | |
<!--*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=== | ||
Line 86: | Line 85: | ||
'''Literature references:'''<br> | '''Literature references:'''<br> | ||
− | + | [http://www.ncbi.nlm.nih.gov/pubmed/15932991 '''Pubmed''' : Jiang, H., Wood, K.V., Morgan, J.A., 2005. Metabolic Engineering of the Phenylpropanoid Pathway in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 71, 2962–2969] | |
'''Database references:'''<br> | '''Database references:'''<br> | ||
− | + | [http://www.ncbi.nlm.nih.gov/nuccore/AX366866 '''GenBank''': Sequence 18 from Patent WO0208402] | |
<!--*[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/P11544 '''Uniprot''': Phenylalanine/tyrosine ammonia-lyase] | ||
<!--*[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?]--> |
Revision as of 22:38, 26 September 2012
phenylalanine ammonia lyase (PAL) coding region
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 2090
Illegal BamHI site found at 352
Illegal XhoI site found at 403
Illegal XhoI site found at 466
Illegal XhoI site found at 484
Illegal XhoI site found at 562
Illegal XhoI site found at 763
Illegal XhoI site found at 1006
Illegal XhoI site found at 1753 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 922
Illegal NgoMIV site found at 1168
Illegal NgoMIV site found at 1336
Illegal NgoMIV site found at 1479
Illegal NgoMIV site found at 1813 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 463
Illegal BsaI site found at 793
Illegal BsaI site found at 799
Illegal BsaI.rc site found at 1924
Illegal SapI site found at 753
Plasmid (template for PCR) provided by John A. Morgan, School of Chemical Engineering, Purdue University, West Lafayette, Indiana, USA
http://www.ncbi.nlm.nih.gov/nuccore/AX366866
PMID: 15932991
Keywords:
Coumaryol-CoA, Coumaroyl-Coenzyme A, Xanthohumol, Biosynthesis, 4-coumarate-coenzyme A ligase
Abbreviations:
PAL = Phenylalanine Ammonia Lyase
Design Notes
Related BioBrick:
Quality control measures:
Part was totally sequenced
Backbone:
Backbone name: pSB1C3
Resistance: Cp
Protein coding:
Protein: Phenylalanine Ammonia Lyase
Enzymatic activity: EC-number 4.3.1.25
Cytotoxicity:
Safety notes:
Intellectual property:
Corresponding part author/authors:
Source
Source:
- Plasmid: pKS2µHyg-PAL-4CL-CHS, provided by John A. Morgan, Purdue University, USA
Organism:
- Genesequence derived from Rhodosporidium toruloides'
References
Literature references:
[http://www.ncbi.nlm.nih.gov/pubmed/15932991 Pubmed : Jiang, H., Wood, K.V., Morgan, J.A., 2005. Metabolic Engineering of the Phenylpropanoid Pathway in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 71, 2962–2969]
Database references:
[http://www.ncbi.nlm.nih.gov/nuccore/AX366866 GenBank: Sequence 18 from Patent WO0208402]
[http://www.uniprot.org/uniprot/P11544 Uniprot: Phenylalanine/tyrosine ammonia-lyase]