Eubacterium acidaminophilum

Glycine reductase selenoprotein B Energy metabolism Eubacterium acidaminophilum 101-103... 

Eubacterium acidaminophilum not only reductively deaminates glycine to ammonia and acetate but also expresses enzymes capable of reductively deaminating sarcosine and betaine when cells are cultured in the presence of formate (Hormann and Andreesen 1989). One would expect that the enzymes catalyzing the latter two reactions might be similar to GR. In fact, the substrate-specific protein B for sarcosine reductase was purified and found to be similar to GR protein B from C. sticklandii (Meyer et al. 1995). Apparently, this organism has evolved means to use different amino acids as electron acceptors and preferentially expresses each in response to conditions in the environment. 

Dietrichs D, Meyer M, Rieth M, Andreesen JR. 1991. Interaction of selenoprotein PA and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale. J Bacteriol 173 5983-91. 

Hermann K, Andreesen JR. 1989. Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase. Arch Microbiol 153 50-9. 

Meyer M, Granderath K, Andreesen JR. 1995. Purification and characterization of protein PB of betaine reductase and its relationship to the corresponding proteins glycine reductase and sarcosine reductase from Eubacterium acidaminophilum. Eur J Biochem 234 184-91. 

Wagner M, Sonntag D, Grimm R, et al. 1999. Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis. Eur J Biochem 260 38-49. 

Zindel U., Freudenberg W., Rieth M., Andreesen 1. R., SchneU L, and Widdel F. (1988) Eubacterium acidaminophilum sp. nov., a versatile amino acid-degrading anaerobe producing or utilizing H2 or formate description and enzymatic studies. Arch. Microbiol. 150, 254-266. 

Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J Biol Chem 276 24557-24564. 

---