Gully N J, Rogers A H
Department of Dentistry, University of Adelaide, Australia.
FEMS Microbiol Lett. 1996 Jun 1;139(2-3):209-13. doi: 10.1111/j.1574-6968.1996.tb08204.x.
Eikenella corrodens 33EK(L), a clinical isolate, was assayed for its ability to utilise amino acids as substrates in the reduction of nitrate to nitrite. The metabolism of proline, glutamate, serine and glutamine was found to result in relatively high rates of nitrate reduction. The ability of cells to metabolise these amino acids from a variety of small peptides was also determined. E. corrodens was found to possess a relatively specific proline aminopeptidase as well as a putative carboxypeptidase activity for glutamate. Energy production in this organism appears to be via oxidative deamination of these key amino acids linked to a respiratory chain, with nitrate acting as the ultimate electron acceptor.
迟缓埃肯菌33EK(L),一株临床分离株,被检测了利用氨基酸作为底物将硝酸盐还原为亚硝酸盐的能力。研究发现脯氨酸、谷氨酸、丝氨酸和谷氨酰胺的代谢导致相对较高的硝酸盐还原率。还测定了细胞从各种小肽中代谢这些氨基酸的能力。发现迟缓埃肯菌具有相对特异性的脯氨酸氨基肽酶以及谷氨酸的假定羧肽酶活性。该生物体中的能量产生似乎是通过这些与呼吸链相连的关键氨基酸的氧化脱氨作用,硝酸盐作为最终电子受体。