Part:BBa_K1129045
Phenylalanine ammonia lyase under pTET constitutive promoter
Const.+rbs+PAL
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 7
Illegal NheI site found at 30 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 2151
Illegal BamHI site found at 413
Illegal XhoI site found at 464
Illegal XhoI site found at 527
Illegal XhoI site found at 545
Illegal XhoI site found at 623
Illegal XhoI site found at 824
Illegal XhoI site found at 1067
Illegal XhoI site found at 1814 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 983
Illegal NgoMIV site found at 1229
Illegal NgoMIV site found at 1397
Illegal NgoMIV site found at 1540
Illegal NgoMIV site found at 1874 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 524
Illegal BsaI site found at 854
Illegal BsaI site found at 860
Illegal BsaI.rc site found at 1985
Illegal SapI site found at 814
Phenylalanine Ammonia Lyase (PAL) is an enzyme responsible for the conversion of the amino acid phenylalanine to trans-cinnamic acid. PAL is the first committed enzyme in the Phenylpropanoid pathway and is therefore involved in lignin degradation. PAL’s can be found in plants, fungi, and bacteria and it has a molecular mass in the range of 270-330 kDa. The deaminating action of PAL is conserved among the ammonia Lyase family that includes Histadine Ammonia Lyase, and Tyrosine Ammonia Lyase.
Useful resources
1) http://en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase
2) http://www.genome.jp/kegg-bin/show_pathway?map00940
3) http://www.uniprot.org/uniprot/P25872
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