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The Post-Polyketide Synthase Modification Mechanism in Hitachimycin Biosynthesis.

Fumitaka Kudo1, Kazuma Tsuboi1, Mutsumi Ikezaki1

  • 1Department of Chemistry, Tokyo Institute of Technology, 2-12-1 Meguro-ku, O-okayama, Tokyo, 152-8551, Japan.

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|June 7, 2024
PubMed
Summary

Researchers elucidated the post-polyketide synthase (PKS) modification pathway for hitachimycin biosynthesis. Gene inactivation revealed a key intermediate and identified enzymes involved in constructing this bicyclic macrolactam antibiotic.

Keywords:
Streptomycesbiosynthesishitachimycinmacrolactampolyketidepost-polyketide synthase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Biosynthesis

Background:

  • Hitachimycin is a bicyclic macrolactam antibiotic featuring (S)-β-phenylalanine (β-Phe).
  • While initial steps involving β-amino acids and polyketide synthases (PKSs) are understood, the post-PKS modifications forming hitachimycin's unique structure are unknown.

Purpose of the Study:

  • To investigate the post-PKS modification mechanism in hitachimycin biosynthesis.
  • To identify the specific genes and enzymes responsible for constructing the bicyclic structure.

Main Methods:

  • Inactivation of six putative post-PKS modification genes (hitM1-hitM6) in Streptomyces scabrisporus.
  • Analysis of accumulated intermediates in gene knockout strains.
  • In vitro enzymatic assays using purified enzymes and intermediates.

Main Results:

  • Deletion of hitM4 led to accumulation of an all-trans-2,4,6,8,18-pentaene macrolactam, identified as an early post-PKS intermediate.
  • Deletion of hitM1 resulted in 10-O-demethyl-10-oxohitachimycin (M1-A).
  • Enzymatic studies showed HitM1 (a reductase) and HitM6 (a methyltransferase) are crucial for converting M1-A to hitachimycin.

Conclusions:

  • A plausible post-PKS modification pathway for hitachimycin biosynthesis has been proposed.
  • HitM4 is involved in an early step, while HitM1 and HitM6 catalyze later modifications, including reduction and methylation, to form the final antibiotic structure.