6.3.2.31: coenzyme F420-0:L-glutamate ligase
This is an abbreviated version!
For detailed information about coenzyme F420-0:L-glutamate ligase, go to the full flat file.
Reaction
Synonyms
bifunctional F420 biosynthesis protein FbiB, BQ2027_MB3290, CofE, CofE-AF, F420-0:gamma-glutamyl ligase, FbiB, MJ0768
ECTree
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General Information
General Information on EC 6.3.2.31 - coenzyme F420-0:L-glutamate ligase
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physiological function
both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
physiological function
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
physiological function
in vitro, MtbFbiB synthesizes side chains containing up to seven glutamate residues if cofactor F420 is presented to the enzyme in a two-electron reduced state (F420H2). The polyglutamylation process requires the assistance of F420-dependent glucose-6-phosphate dehydrogenase (Fgd) which reduces F420 to F420H2. Starting with F420-0H2, the amino-terminal domain of FbiB may build F420-2H2, which is then transferred to the carboxy-terminal domain for further glutamylation. F420-2H2 modifies the carboxy-terminal domain structurally to accommodate longer glutamyl chains
physiological function
Mycobacterium tuberculosis variant bovis ATCC BAA-935
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both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
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physiological function
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FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
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physiological function
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FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
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physiological function
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in vitro, MtbFbiB synthesizes side chains containing up to seven glutamate residues if cofactor F420 is presented to the enzyme in a two-electron reduced state (F420H2). The polyglutamylation process requires the assistance of F420-dependent glucose-6-phosphate dehydrogenase (Fgd) which reduces F420 to F420H2. Starting with F420-0H2, the amino-terminal domain of FbiB may build F420-2H2, which is then transferred to the carboxy-terminal domain for further glutamylation. F420-2H2 modifies the carboxy-terminal domain structurally to accommodate longer glutamyl chains
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