ArticleMicrobial cell factories2021
Pyridoxal-5'-phosphate-dependent enzyme GenB3 Catalyzes C-3',4'-dideoxygenation in gentamicin biosynthesis.
Article in Microbial cell factories, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Improving activity of GenB3 and GenB4 in gentamicin dideoxygenation biosynthesis by semi-rational engineering.Microbial cell factories · 2025Article
- Blasticidin S Biosynthesis Involves a Unique Interplay between a Radical SAM Dehydratase, a Transaminase and an ATP-Grasp Ligase in Order to Avoid a Futile Cycle.ACS catalysis · 2025Article
- Recent advances in the biosynthesis and production optimization of gentamicin: A critical review.Synthetic and systems biotechnology · 2025Review
- Recent advances in the biosynthetic pathway and structural modification of gentamicin.Frontiers in microbiology · 2025Review
- Men with oligozoospermia had lower level of seminal plasma pyridoxine compared to normozoospermic men.Heliyon · 2022Article
- (Meta)Genomic Analysis Reveals Diverse Energy Conservation Strategies Employed by Globally DistributedmSystems · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
backgroundThe C-3',4'-dideoxygenation structure in gentamicin can prevent deactivation by aminoglycoside 3'-phosphotransferase (APH(3')) in drug-resistant pathogens. However, the enzyme catalyzing the dideoxygenation step in the gentamicin biosynthesis pathway remains unknown.
resultsHere, we report that GenP catalyzes 3' phosphorylation of the gentamicin biosynthesis intermediates JI-20A, JI-20Ba, and JI-20B. We further demonstrate that the pyridoxal-5'-phosphate (PLP)-dependent enzyme GenB3 uses these phosphorylated substrates to form 3',4'-dideoxy-4',5'-ene-6'-oxo products. The following C-6'-transamination and the GenB4-catalyzed reduction of 4',5'-olefin lead to the formation of gentamicin C. To the best of our knowledge, GenB3 is the first PLP-dependent enzyme catalyzing dideoxygenation in aminoglycoside biosynthesis.
conclusionsThis discovery solves a long-standing puzzle in gentamicin biosynthesis and enriches our knowledge of the chemistry of PLP-dependent enzymes. Interestingly, these results demonstrate that to evade APH(3') deactivation by pathogens, the gentamicin producers evolved a smart strategy, which utilized their own APH(3') to activate hydroxyls as leaving groups for the 3',4'-dideoxygenation in gentamicin biosynthesis.
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