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Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin.
TLDR
In vitro assay of the overexpressed enzyme revealed that BtrN catalyzed the oxidation of DOIA under the strictly anaerobic conditions along with consumption of an equimolar amount of SAM to produce 5'-deoxyadenosine, methionine, and 3-amino-2,3-dideoxy-scyllo-inosose (amino -DOI).
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Butirosin-biosynthetic gene cluster from Bacillus circulans.
TLDR
The gene cluster found so far was determined to be a part of the butirosin biosynthetic gene cluster, which is an interesting 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotic produced by non-actinomycete Bacilli.
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Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy.
TLDR
Comparison of signals derived from a [4Fe-4S] center of BtrN incubated with various combinations of products (5'-deoxyadenosine, l-methionine, and amino-DOI) and substrates (SAM and DOIA) indicated that the EPR signals observed during the reaction were derived from free BTrN, a Btrn-SAM complex, and a BTRN-SAM-DOIA complex.
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A new family of glucose-1-phosphate/glucosamine-1-phosphate nucleotidylyltransferase in the biosynthetic pathways for antibiotics.
TLDR
It appears therefore that gene clusters for antibiotic biosynthesis provide their own nucleotidylyltransferases, and the BtrD homologues are among the secondary metabolism specific enzymes.
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Biosynthetic enzymes for the aminoglycosides butirosin and neomycin.
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Involvement of Two Distinct N‐Acetylglucosaminyltransferases and a Dual‐Function Deacetylase in Neomycin Biosynthesis
TLDR
Neomycin is one of the clinically important 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics, which specifically interact with bacterial rRNA and inhibit protein synthesis, and neoD was presumed to catalyze N-acetylglucosaminylation of DOS.
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Cloning of the biosynthetic gene cluster for naphthoxanthene antibiotic FD-594 from Streptomyces sp. TA-0256
TLDR
To clarify the involvement of pnx genes in the FD-594 biosynthesis, a glycosyltransferase, PnxGT2, and a methyltransferase were characterized enzymatically with the recombinant proteins expressed in Escherichia coli to confirm that the PnXGT2 reaction product was the expected regiospecifically Glycosylated compound.
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Biosynthesis of natural products containing β-amino acids.
TLDR
This review surveys the known bioactive β-amino acid-containing natural products including nonribosomal peptides, macrolactam polyketides, and nucleoside-β-AMino acid hybrids and the mechanisms of β-Amino acid incorporation into natural products.
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Molecular cloning of the gene for the key carbocycle-forming enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics and its comparison with dehydroquinate synthase.
TLDR
The previous proposal for the similarity of 2-deoxy-scyllo-inosose synthase to dehydroquinate synthase has been confirmed on the basis of their amino acid sequences and comparison of the BtrC sequence with those of biosynthetic enzymes for other related microbial products is discussed.
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Cloning of the Pactamycin Biosynthetic Gene Cluster and Characterization of a Crucial Glycosyltransferase Prior to a Unique Cyclopentane Ring Formation
TLDR
The enzymatic activity of the PctL protein clearly confirmed that the present identified gene cluster is for the biosynthesis of pactamycin, and a glycosylation prior to cyclopentane ring formation was proposed to be a general strategy in the biosynthetic of the structurally related cyclopency containing compounds.
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