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Literature summary extracted from

  • Dong, C.; Huang, F.; Deng, H.; Schaffrath, C.; Spencer, J.B.; O'Hagan, D.; Naismith, J.H.
    Crystal structure and mechanism of a bacterial fluorinating enzyme (2004), Nature, 427, 561-565.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.63 gene flA, DNA sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) and in strain B834(DE3), the latter results in the selenomethionine labeled enzyme Streptomyces cattleya

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.63 purified recombinant wild-type and selenomethionine labelled enzyme with bound S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.9 A resolution, structure modelling of monomers a and b Streptomyces cattleya

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.63 34402
-
 6 * 34402, (alpha,beta)3, recombinant enzyme, ESI-MS mass spectrometry Streptomyces cattleya

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.63 S-adenosyl-L-methionine + fluoride Streptomyces cattleya
-
 5'-deoxy-5'-fluoroadenosine + L-methionine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.63 Streptomyces cattleya
-
 gene flA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.63 recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Streptomyces cattleya

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.63 S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine substrate binding structure involving F156, S158, Y177, and T80, nucleophilic substitution reaction mechanism Streptomyces cattleya
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.63 culture condition:fluoride-grown cell
-
 Streptomyces cattleya
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.63 S-adenosyl-L-methionine + fluoride
-
 Streptomyces cattleya 5'-deoxy-5'-fluoroadenosine + L-methionine
-
 ?
2.5.1.63 S-adenosyl-L-methionine + fluoride highly specific for S-adenosyl-L-methionine, which is tightly bound to the enzyme at the interface between C-terminal domain of one monomer and the N-terminal domain of the neighbouring monomer Streptomyces cattleya 5'-deoxy-5'-fluoroadenosine + L-methionine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.63 hexamer 6 * 34402, (alpha,beta)3, recombinant enzyme, ESI-MS mass spectrometry Streptomyces cattleya
2.5.1.63 More the N-terminal domain has a central seven-stranded beta-sheet, which combines parallel and antiparallel strands sandwiched between alpha-helices, the C-terminal domain is composed of a five- and a four-stranded antiparallel beta-sheet Streptomyces cattleya

Synonyms

EC Number Synonyms Comment Organism
2.5.1.63 5'-deoxy-5'-fluoroadenosine synthase
-
 Streptomyces cattleya
2.5.1.63 5'-FDAS
-
 Streptomyces cattleya
2.5.1.63 fluorination enzyme
-
 Streptomyces cattleya

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.63 37
-
 assay at Streptomyces cattleya

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.63 0.0012
-
 fluoride
-
 Streptomyces cattleya
2.5.1.63 0.074
-
 S-adenosyl-L-methionine
-
 Streptomyces cattleya
2.5.1.63 2
-
 fluoride
-
 Streptomyces cattleya

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.63 7.9
-
 assay at Streptomyces cattleya