DNA

Part:BBa_K5443001

Designed by: Nick Coleman, Carmen Hawthorne   Group: iGEM24_MacquarieUni   (2024-09-27)


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).


Figure 1. TAL-catalysed conversion of tyrosine to p-coumaric acid.
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


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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Parameters
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