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Literature summary extracted from

  • Graham, D.E.; Xu, H.; White, R.H.
    Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis (2003), Arch. Microbiol., 180, 455-464 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.147 Dithionite after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold Mycolicibacterium smegmatis
4.3.1.32 Dithionite after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.147 Fe2+ after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold Mycolicibacterium smegmatis
4.3.1.32 Fe2+ after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.147 40000
-
 SDS-PAGE Methanocaldococcus jannaschii
2.5.1.147 88000
-
 SDS-PAGE Mycolicibacterium smegmatis
4.3.1.32 42000
-
 SDS-PAGE Methanocaldococcus jannaschii
4.3.1.32 88000
-
 SDS-PAGE Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.1.32 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine Mycolicibacterium smegmatis the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32) 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.147 Methanocaldococcus jannaschii Q58826
-
-
2.5.1.147 Methanocaldococcus jannaschii DSM 2661 Q58826
-
-
2.5.1.147 Mycolicibacterium smegmatis
-
-
-
4.3.1.32 Methanocaldococcus jannaschii Q57888
-
-
4.3.1.32 Methanocaldococcus jannaschii DSM 2661 Q57888
-
-
4.3.1.32 Mycolicibacterium smegmatis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.147 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
 ?
2.5.1.147 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32) Mycolicibacterium smegmatis 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
 ?
2.5.1.147 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii DSM 2661 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
 ?
4.3.1.32 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?
4.3.1.32 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32) Mycolicibacterium smegmatis 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?
4.3.1.32 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii DSM 2661 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5'-deoxyadenosine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.147 cofH
-
 Methanocaldococcus jannaschii
2.5.1.147 fbiC gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32). In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide Mycolicibacterium smegmatis
2.5.1.147 MjCofH
-
 Methanocaldococcus jannaschii
4.3.1.32 cofG
-
 Methanocaldococcus jannaschii
4.3.1.32 fbiC gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32). In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide Mycolicibacterium smegmatis
4.3.1.32 MjCofG
-
 Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.147 70
-
 activity is not significantly reduced during incubations at 70°C Mycolicibacterium smegmatis
4.3.1.32 70
-
 activity is not significantly reduced during incubations at 70°C Mycolicibacterium smegmatis

Expression

EC Number Organism Comment Expression
2.5.1.147 Mycolicibacterium smegmatis cloning of the fused Mycobacterium smegmatis fbiC gene and heterologous expression of the bifunctional MsFbiC in Escherichia coli additional information
2.5.1.147 Methanocaldococcus jannaschii heterologous expression in Escherichia coli and functional characterization in vitro. MjCofH is expressed as a fusion protein with an N-terminal polyhistidine tag. The His-tagged protein is strongly expressed in Escherichia coli but is slightly more soluble than the untagged protein additional information
4.3.1.32 Mycolicibacterium smegmatis cloning of the fused Mycobacterium smegmatis fbiC gene and heterologous expression of the bifunctional MsFbiC in Escherichia coli additional information
4.3.1.32 Methanocaldococcus jannaschii heterologous expression in Escherichia coli and functional characterization in vitro. MjCofG is substantially soluble in cell-free extract additional information

General Information

EC Number General Information Comment Organism
2.5.1.147 metabolism the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420 Methanocaldococcus jannaschii
2.5.1.147 metabolism the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420. In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide, the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32) Mycolicibacterium smegmatis
4.3.1.32 metabolism the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420. In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide, the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32) Mycolicibacterium smegmatis
4.3.1.32 metabolism the enzyme produces the 7,8-didemethyl-8-hydroxy-5-deazariboflavin precursor of the redox cofactor coenzyme F420. The precursor of the redox cofactor coenzyme F420 Methanocaldococcus jannaschii