Part:BBa_K5443003

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

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]