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Literature summary for 2.1.1.308 extracted from

  • Allen, K.D.; Wang, S.C.
    Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis (2014), Arch. Biochem. Biophys., 543, 67-73.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.308

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Rosetta 2 (DE3) pLysS cells as a hexahistidine-tagged protein. The recombinant proteins are found exclusively in inclusion bodies. After refolding and concentration, the protein is reconstituted with additional iron and sulfide to maximize cluster formation Streptomyces wedmorensis

Protein Variants

Protein Variants Comment Organism
C282A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
C282A/C286A/C289A the triple-variant is very unstable and precipitated during purification and subsequent manipulation for experiments. It completely lacks the [4Fe-4S]+1 cluster Streptomyces wedmorensis
C286A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
C289A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
additional information site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation Streptomyces wedmorensis

Metals/Ions

Metals/Ions Comment Organism Structure
[4Fe-4S] cluster the [4Fe-4S] cluster undergoes a transition between a +2 resting state and a +1 active state. Site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation Streptomyces wedmorensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60400
-
 10 * or 12 * 60400, SDS-PAGE Streptomyces wedmorensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate Streptomyces wedmorensis the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces wedmorensis Q56184
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptomyces wedmorensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate
-
 Streptomyces wedmorensis 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin Streptomyces wedmorensis 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?

Subunits

Subunits Comment Organism
multimer 10 * or 12 * 60400, SDS-PAGE Streptomyces wedmorensis

Synonyms

Synonyms Comment Organism
fom3
-
 Streptomyces wedmorensis

Cofactor

Cofactor Comment Organism Structure
Cobalamin
-
 Streptomyces wedmorensis

General Information

General Information Comment Organism
metabolism the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin Streptomyces wedmorensis