Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme.

@article{Kamigiri1992StudiesOT,
  title={Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme.},
  author={Kazuma Kamigiri and Tomomi Hidaka and Satoshi Imai and Takeshi Murakami and Haruo Seto},
  journal={The Journal of antibiotics},
  year={1992},
  volume={45 5},
  pages={
          781-7
        }
}
An enzymatic activity catalyzing P-methylation of N-acetyldemethylphosphinothricin, a biosynthetic intermediate of the herbicide bialaphos, was detected in a cell extract of Streptomyces hygroscopicus SF-1293, a bialaphos producing organism. The gene coding for this P-methylation enzyme in the bialaphos biosynthetic gene cluster was also expressed in Streptomyces lividans. The methyl donor of the reaction was determined to be methylcobalamin. The P-methylation enzyme utilized both N… 
Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate
TLDR
PnPy decarboxylase drives the unfavorable forward reaction to form PnPy catalyzed by PEP phosphomutase and is suggested to be essential to C-P compound biosynthesis.
Studies on the biosynthesis of fosfomycin. 4. The biosynthetic origin of the methyl group of fosfomycin.
TLDR
By bioconversion experiments using two FM non-producing mutants of Streptomyces wedmorensis, NP-7 and A16, it is shown that the epoxide ring of FM was formed by dehydrogenation of 2-hydroxypropylphosphonic acid (HPP)10'11*.
Biosynthetic pathways and enzymes involved in the production of phosphonic acid natural products.
TLDR
The biosynthesis of FM is reviewed, which includes a recent breakthrough to find a missing link in the biosynthetic pathway that had been a mystery for a quarter-century and the genome mining of phosphonate natural products using the biosynthesis gene encoding an enzyme that catalyzes C-P bond formation.
Cobalamin-dependent radical S-adenosyl-l-methionine enzymes in natural product biosynthesis.
TLDR
The investigation of cobalamin (Cbl)- and radical S-adenosyl-l-methionine (SAM)-dependent enzymes found in natural product biosynthesis to date is summarized and some possibilities for the future are suggested.
GenK-catalyzed C-6' methylation in the biosynthesis of gentamicin: isolation and characterization of a cobalamin-dependent radical SAM enzyme.
TLDR
In vitro activity of GenK, a Cbl-dependent radical SAM enzyme that methylates an unactivated sp(3) carbon during the biosynthesis of gentamicin, an aminoglycoside antibiotic, is demonstrated and one mechanistic possibility for the GenK reaction can be ruled out.
In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea.
TLDR
The activity of the P-methyltransferase enzyme, PhpK, is demonstrated from the phosalacine producer Kitasatosporaphosalacinea to give rise to the only carbon-phosphorus-carbon linkage known to occur in nature.
Nucleotide sequence of fortimicin KL1 methyltransferase gene isolated from Micromonospora olivasterospora, and comparison of its deduced amino acid sequence with those of methyltransferases involved in the biosynthesis of bialaphos and fosfomycin.
TLDR
PnAA was directly methylated by a nucleophilic attack of the methyl anion derived from methylcobalamin catalyzed by PnAA methyltransferase, and the nucleotide sequences of the genes encoding P-methyltransferase were determined.
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References

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Biochemical mechanism of C-P bond formation of bialaphos: Use of gene manipulation for the analysis of the C-P bond formation step.
TLDR
Biochemical analysis of a new BA non-producing mutant NP71 indicated that NP71 was defective in the formation of carboxyphosphonoenolpyruvate (CPEP), while NP213 lacked the enzyme CPEP phosphonomutase, which catalyzed the intramolecular rearrangement of CPEP.
Studies on the biosynthesis of bialaphos (SF-1293). 2. Isolation of the first natural products with a C-P-H bond and their involvement in the C-P-C bond formation.
TLDR
2-Phosphinomethylmalic acid synthase catalyzes the condensation of phosphinopyruvic acid, an analog of oxalacetic acid, and acetyl-CoA to form PMM, which is very similar to (R)-citrate synthase of Clostridium in the inhibition pattern by sulfhydryl compounds, its metal ion requirement and stereospecificity.
Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation
An enzyme catalyzing the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA) was isolated from the cell extract of a mutant (NP71) of Streptomyces
The bialaphos biosynthetic genes of Streptomyces hygroscopicus: cloning and analysis of the genes involved in the alanylation step.
TLDR
Results suggest that multiple genes are involved in the alanylation step in the biosynthesis of a herbicide, bialaphos which is produced by Streptomyces hygroscopicus, and are located between the genes which code for phosphinomethylmalic acid synthase and demethylphosphinothricin acetyltransferase in the cluster.
Biosynthetic incorporation of methyl groups into fortimicins.
TLDR
It was reported that cobalamin showed a stimulatory effect on fortimicin A production and had much less effect on the fortimICin B production, which indicated that cobalt dependent methylation was required in the biosynthesis of fortimics A and besides methyl group of methylcobalamin was directly incorporated into Fortimicins, particularly, fortimiin A.
Replacement of Streptomyces hygroscopicus genomic segments with in vitro altered DNA sequences.
TLDR
A method for gene replacement in Streptomyces hygroscopicus which permits introduction of an in vitro derived mutation carried on a plasmid into the chromosome and will enable isogenic mutants of known genes and to identify new genes encoded on a cloned fragment to be obtained.
Thiostrepton-induced gene expression in Streptomyces lividans
TLDR
The thiostrepton-inducible tipA promoter should be a valuable tool for expression studies in streptomycetes and is cloned into a promoter probe vector, pIJ486.
Cloning of antibiotic resistance and nutritional genes in streptomycetes
Methodology which allows consistent shotgun cloning of streptomycete genes is presented. Parameters that increase transformation efficiency of Streptomyces lividans 66 were adjusted to generate
THE CHEMISTRY OF Co(I) DERIVATIVES OF VITAMIN B12 AND OF RELATED CHELATES
  • G. Schrauzer
  • Chemistry
    Annals of the New York Academy of Sciences
  • 1969
The main points of the present review can be summarized as follows:
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