Cc. Chien et al., TAURINE-SULFUR ASSIMILATION AND TAURINE-PYRUVATE AMINOTRANSFERASE ACTIVITY IN ANAEROBIC-BACTERIA, Applied and environmental microbiology, 63(8), 1997, pp. 3021-3024
We demonstrated the ability of strictly fermentative, as well as facul
tatively fermentative, bacteria to assimilate sulfonate sulfur for gro
wth. Taurine (2-aminoethanesulfonate) can be utilized by Clostridium p
asteurianum C1 but does not support fermentative growth of two Klebsie
lla spp. and two different Clostridium spp. However, the latter are ab
le to assimilate the sulfur of a variety of other sulfonates (e.g., cy
steate, 3-sulfopyruvate, and 3-sulfolactate) anaerobically. A novel ta
urine-pyruvate aminotransferase activity was detected in cell extracts
of C. pasteurianum C1 grown with taurine as the sole sulfur source. T
his activity was not detected in extracts of other bacteria examined,
in C. pasteurianum C1 grown with sulfate or sulfite as the sulfur sour
ce, or in a Klebsiella isolate assimilating taurine-sulfur by aerobic
respiration. More common aminotransferase activities (e.g., with aspar
tate or glutamate as the amino donor and pyruvate, oxalacetate, or alp
ha-ketoglutarate as the amino acceptor) were present, no matter what s
ulfur source was used for growth. Partial characterization of the taur
ine-pyruvate aminotransferase revealed an optimal temperature of 37 de
grees C and a broad optimal pH range of 7.5 to 9.5.