Roseiflexus castenholzii is a heterotrophic, thermophilic, filamentous anoxygenetic phototroph (FAP) bacterium. This species is in one of two genera of FAPs that lack chlorosomes. R. castenholzii was first isolated from red-colored bacterial mats located Nakabusa hot springs in Japan. Because this organism is a phototroph, it utilizes photosynthesis to fix carbon dioxide and build biomolecules. R. castenholzii has three photosynthetic complexes: light-harvesting, reaction center, and light-harvesting - reaction center.
The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. The bi-functional enzyme catalyzes NADPH-dependent reduction of malonyl-CoA to 3-HP, an important metabolic intermediate and platform chemical, from biomass.
Here you can see the cryo-EM structure of the bi-functional malonyl-CoA reductase from Roseiflexus castenholzii (PDB code: 8HI4)
#molecularart ... #immolecular ... #enzyme ... #bifunctional ... #malonyl ... #reductase ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. The bi-functional enzyme catalyzes NADPH-dependent reduction of malonyl-CoA to 3-HP, an important metabolic intermediate and platform chemical, from biomass.
Here you can see the cryo-EM structure of the bi-functional malonyl-CoA reductase from Roseiflexus castenholzii (PDB code: 8HI4)
#molecularart ... #immolecular ... #enzyme ... #bifunctional ... #malonyl ... #reductase ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
