Difference between revisions of "Part:BBa K5443001"
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This enzyme from <i>Saccharothrix espanaensis</i> catalyses the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin (Fig. 1). This reaction is critical as it initiates the entry of tyrosine into the phenylpropanoid pathway. Tyrosine ammonia-lyase (TAL) is a member of the aromatic amino acid lyase family, which also includes phenylalanine (PAL) and histidine ammonia-lyases (HAL). TAL is highly specific for L-tyrosine, catalysing its non-oxidative deamination, making a trans-2,3-unsaturated substituted propenoic acid and ammonia. | This enzyme from <i>Saccharothrix espanaensis</i> catalyses the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin (Fig. 1). This reaction is critical as it initiates the entry of tyrosine into the phenylpropanoid pathway. Tyrosine ammonia-lyase (TAL) is a member of the aromatic amino acid lyase family, which also includes phenylalanine (PAL) and histidine ammonia-lyases (HAL). TAL is highly specific for L-tyrosine, catalysing its non-oxidative deamination, making a trans-2,3-unsaturated substituted propenoic acid and ammonia. | ||
| − | This part builds on the work of earlier iGEM teams, who contributed TAL Parts as follows: [https://parts.igem.org/Part: | + | This part builds on the work of earlier iGEM teams, who contributed TAL Parts as follows: [https://parts.igem.org/Part:BBa_I742142 BBa_I742142], [https://parts.igem.org/Part:BBa_K2906011 BBa_K2906011], and [https://parts.igem.org/Part:BBa_K1197011 BBa_K1197011]. |
| − | We showed that the <i>Saccharothrix</i> TAL enzyme was functional in <i>E. coli<i> as part of a vanillin biosynthetic pathway, as evidenced by production of p-coumaric acid from tyrosine in one clone, named pMC3C-11 (see LC-MS data in the [https://parts.igem.org/Part:BBa_K5443001:Experience experience] page). | + | We showed that the <i>Saccharothrix</i> TAL enzyme was functional in <i>E. coli</i> as part of a vanillin biosynthetic pathway, as evidenced by production of p-coumaric acid from tyrosine in one clone, named pMC3C-11 (see LC-MS data in the [https://parts.igem.org/Part:BBa_K5443001:Experience experience] page). |
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Latest revision as of 12:49, 2 October 2024
Tyrosine ammonia lyase (TAL) - (SAM8)
This enzyme from Saccharothrix espanaensis catalyses the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin (Fig. 1). This reaction is critical as it initiates the entry of tyrosine into the phenylpropanoid pathway. Tyrosine ammonia-lyase (TAL) is a member of the aromatic amino acid lyase family, which also includes phenylalanine (PAL) and histidine ammonia-lyases (HAL). TAL is highly specific for L-tyrosine, catalysing its non-oxidative deamination, making a trans-2,3-unsaturated substituted propenoic acid and ammonia.
This part builds on the work of earlier iGEM teams, who contributed TAL Parts as follows: BBa_I742142, BBa_K2906011, and BBa_K1197011.
We showed that the Saccharothrix TAL enzyme was functional in E. coli as part of a vanillin biosynthetic pathway, as evidenced by production of p-coumaric acid from tyrosine in one clone, named pMC3C-11 (see LC-MS data in the experience page).
This reaction represents the first step in our vanillin synthesis pathway, where the enzyme Tyrosine Ammonia Lyase (TAL) converts Tyrosine into p-Coumaric Acid.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 484
Illegal AgeI site found at 1095 - 1000COMPATIBLE WITH RFC[1000]