Difference between revisions of "Part:BBa K5443003"

 
 
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4-Hydroxyphenylacetate (HpaBC) 3-hydroxylase (C3H) from <i>E. coli</i> is an alternative enzyme variant to Sam5 to catalyse the hydroxylation of 4-coumaric acid to yield caffeic acid (Fig. 1). This functions as the second step in our vanillin biosynthesis pathway. HpaBC is a two-component flavin adenine dinucleotide (FAD)-dependent monooxygenase that has a broad host range, and acts on a wide range of phenolic compounds. In our vanillin biosynthesis pathway, HpaBC is performing an “unnatural” role in hydroxylating coumarate (p-coumaric acid), since its normal physiological substrate is 4-hydroxyphenylacetate.
  
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This part builds on the work of earlier iGEM teams, who contributed HpaBC Parts as follows: [https://parts.igem.org/Part:BBa_K1124011 BBa_K1124011], [https://parts.igem.org/Part:BBa_K4912001 BBa K4912001], and [https://parts.igem.org/Part:BBa_K4912008 BBa_K4912008].
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<partinfo>BBa_K5443003 short</partinfo>
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HpaBC converts 4-coumaric acid to caffeic acid, adding the caffeic hydroxyl group necessary for subsequent modifications in the pathway&#8203;&#8203;.
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<figure>
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    <img src=" https://static.igem.wiki/teams/5443/c3h-reaction.jpg" style="width:600px;height:auto">
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    <figcaption>
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        <b>Figure 1. C3H-catalysed conversion of p-coumaric acid to caffeic acid.</b><br>
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        <i>This reaction represents the second step in our vanillin synthesis pathway. The C3H enzyme HpaBC converts coumarate (p-coumaric acid) into caffeic acid.</i>
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    </figcaption>
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Latest revision as of 13:44, 2 October 2024

4-Hydroxyphenylacetate (HpaBC) 3-hydroxylase (C3H) from E. coli is an alternative enzyme variant to Sam5 to catalyse the hydroxylation of 4-coumaric acid to yield caffeic acid (Fig. 1). This functions as the second step in our vanillin biosynthesis pathway. HpaBC is a two-component flavin adenine dinucleotide (FAD)-dependent monooxygenase that has a broad host range, and acts on a wide range of phenolic compounds. In our vanillin biosynthesis pathway, HpaBC is performing an “unnatural” role in hydroxylating coumarate (p-coumaric acid), since its normal physiological substrate is 4-hydroxyphenylacetate.

This part builds on the work of earlier iGEM teams, who contributed HpaBC Parts as follows: BBa_K1124011, BBa K4912001, and BBa_K4912008.


Figure 1. C3H-catalysed conversion of p-coumaric acid to caffeic acid.
This reaction represents the second step in our vanillin synthesis pathway. The C3H enzyme HpaBC converts coumarate (p-coumaric acid) into caffeic 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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]