Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Karl Holdar, Hampus Elofsson, Emil Marklund, Kristoffer Lundmark, Marcus Hong, Lovisa Pettersson, Ken Braech-Andersen, Theodor L??we
Date created: 2013-08-14 11:00:00
Date modified: 2015-05-08 01:08:48
Tyrosine ammonia-lyase (TAL) with RBS
| Types | DnaRegion |
| Roles | Coding CDS |
| Sequences | BBa_K1033000_sequence (Version 1) |
Description
tyrosine ammonia-lyase (TAL) is an enzyme which catalyzes the formation of p-coumaric acid (aka p-hyroxycinnamic acid) from tyrosine. It belongs to the family of ammonia-lyases, enzymes that catalyze the deamination of amino acids [1]. P-coumaric acid is an important precursor in many metabolic pathways. TAL also has a secondary function as a phenylalanine ammonia-lyase (PAL) which catalyses the formation of cinnamic acid. The wild type RsTAL has a preference for tyrosine, however the mutations Met4 -> Ile, Ile325 -> Val and Val409 -> Met, can shift this preference to phenylalanine [2].1.Zhixiong Xue, Michael McCluskey, Keith Cantera, F. Sima Sariaslani, Lixuan Huang (2007) Identification, characterization and functional expression of a tyrosine ammonia-lyase and its mutants from the photosynthetic bacterium Rhodobacter sphaeroides. J Ind Microbiol Biotechnol 34:599-604
2. J.A. Kyndt, T.E. Meyer, M.A Cusanovich, J.J. Van Beeumen (2002) Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Letters 512 240-244
Notes
Earlier in iGEM eucaryot TAL has been used, however we used bacterial TAL for better compatibility with E.coli.Source
Rhodobacter sphaeroides| Sequence Annotation | Location | Component / Role(s) |
| Tyrosine amonia lyase B0034 | 22,1596 4,13 | CDS feature/cds ribosome_entry_site feature/rbs |