Difference between revisions of "Part:BBa K5443001"

Revision as of 07:06, 2 October 2024

Tyrosine ammonia lyase (TAL) - (SAM8)

This enzyme from Saccharothrix espanaensis catalyzes the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin. 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_K1197011, BBa_K1033000, BBa_K2997011. 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 (see LC-MS data from one clone pMQ3C-11).

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 484
Illegal AgeI site found at 1095
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K5443001 short</partinfo>
-This enzyme from Saccharothrix espanaensis catalyzes the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin. This reaction is critical as it initiates the entry of tyrosine into the phenylpropanoid pathway. This part builds on the work of earlier iGEM teams, who contributed TAL Parts as follows: BBa_K1197011, BBa_K1033000, BBa_K2997011. 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 (see LC-MS data from one clone pMQ3C-11).
+This enzyme from Saccharothrix espanaensis catalyzes the deamination of L-tyrosine to 4-coumaric acid, which is the first step in the conversion of tyrosine to vanillin. 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_K1197011, BBa_K1033000, BBa_K2997011. 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 (see LC-MS data from one clone pMQ3C-11).
 https://static.igem.wiki/teams/5443/tal-reaction.jpg