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P450 enzyme KwwB installs Tyr-Trp cross-link on engineered peptides

Nearly the entire leader peptide region tolerated mutations, with only a conserved proline at position -4 proving essential for the reaction.

PR
By Priya Raman · Science Reporter
Oct 8 16:43 ETSource: Bioengineer.org

The wire

  1. 01Researchers report the cyptide synthase KwwB can install a non-native Tyr-C3–Trp-N1 cross-link on engineered precursor peptides and tolerates broad leader-peptide mutation.
  2. 02Enzymatic cross-linking chemistry of this kind underpins macrocyclic peptide production, a route of interest for making more stable and potentially orally available peptide drugs.
  3. 03This is enzymology on engineered substrates, not a therapeutic candidate; translation to any clinical peptide remains distant and unproven.

From the source

Bacterial Enzyme KwwB Forges Unusual Peptide Cross-Links and Shrugs Off Leader Mutations

Researchers have shown that the P450 cyptide synthase KwwB can install a non-native Tyr-C3–Trp-N1 cross-link on engineered precursor peptides and tolerates mutations across nearly its entire leader peptide region, with only a conserved proline at position -4 proving essential.

Read at bioengineer.org
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