Cofactors

Mg(2+).

Reaction Mechanism

There are no Reaction Mechanism for this Enzyme

Reaction Parameters

• Kinetic Parameters

  Organism	KM Value [mM]	Substrate	Comment
  Methanocaldococcus jannaschii	0.006	CTP	apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
  Corynebacterium ammoniagenes	0.0311	FMN	FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C
  Homo sapiens	0.6	roseoflavin mononucleotide	with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
  Streptococcus pneumoniae	11.7	ATP	pH 7.0, 25°C

• Temperature

  There are no reaction parameters information for this Enzyme.

• pH

  There are no reaction parameters information for this Enzyme.

Associated Proteins

Citations

• Functional characterization of the putative FAD synthase from Mycoplasma hyopneumoniae.
• Heterologous Overexpression of Human FAD Synthase Isoforms 1 and 2.
• Cofactors and pathogens: Flavin mononucleotide and flavin adenine dinucleotide (FAD) biosynthesis by the FAD synthase from Brucella ovis.
• Continuous and Discontinuous Approaches to Study FAD Synthesis and Degradation Catalyzed by Purified Recombinant FAD Synthase or Cellular Fractions.
• Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.
• The hidden side of the human FAD synthase 2.
• Purification of Recombinant Human 6His-FAD Synthase (Isoform 2) and Quantitation of FAD/Protein Monomer Ratio by UV-Vis Spectra.
• In silico discovery and biological validation of ligands of FAD synthase, a promising new antimicrobial target.
• In silicodiscovery and biological validation of ligands of FAD synthase, a promising new antimicrobial target
• Mutation of Aspartate 238 in FAD Synthase Isoform 6 Increases the Specific Activity by Weakening the FAD Binding.
• Specific Features for the Competent Binding of Substrates at the FMN Adenylyltransferase Site of FAD Synthase from Corynebacterium ammoniagenes.