TAURINE-SULFUR ASSIMILATION AND TAURINE-PYRUVATE AMINOTRANSFERASE ACTIVITY IN ANAEROBIC-BACTERIA

Citation
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
Citations number
28
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
ISSN journal
00992240
Volume
63
Issue
8
Year of publication
1997
Pages
3021 - 3024
Database
ISI
SICI code
0099-2240(1997)63:8<3021:TAATAA>2.0.ZU;2-E
Abstract
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.