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. | 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. | ||
| − | 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] | + | 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]. |
Revision as of 12:54, 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, K4912001 BBa K4912001, and BBa_K4912008.
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]