Li K, West T P
Olson Biochemistry Laboratories, Department of Chemistry and Biochemistry, South Dakota State University, Brookings, USA.
Lett Appl Microbiol. 1995 Nov;21(5):340-3. doi: 10.1111/j.1472-765x.1995.tb01075.x.
Pyrimidine synthesis in the food spoilage agent Burkholderia cepacia ATCC 25416 was investigated. The five de novo pathway enzymes of pyrimidine biosynthesis were found to be active in B. cepacia ATCC 25416 and growth of this strain on uracil had an effect on the de novo enzyme activities. The in vitro regulation of aspartate transcarbamoylase activity in B. cepacia ATCC 25416 was studies and its activity was inhibited by PP(i), ATP, GTP, CTP and UTP. The enzymes cytidine deaminase, uridine phosphorylase and cytosine deaminase were found to be active in the salvage of pyrimidines in ATCC 25416. Overall, de novo pyrimidine synthesis in B. cepacia ATCC 25416 was regulated at the level of enzyme activity and its pyrimidine salvage enzymes differed from those found in B. cepacia ATCC 17759.
对食品腐败菌洋葱伯克霍尔德菌ATCC 25416中的嘧啶合成进行了研究。发现嘧啶生物合成的五条从头合成途径的酶在洋葱伯克霍尔德菌ATCC 25416中具有活性,并且该菌株在尿嘧啶上的生长对从头合成酶的活性有影响。对洋葱伯克霍尔德菌ATCC 25416中天冬氨酸转氨甲酰酶活性的体外调节进行了研究,其活性受到焦磷酸(PP(i))、ATP、GTP、CTP和UTP的抑制。发现胞苷脱氨酶、尿苷磷酸化酶和胞嘧啶脱氨酶在ATCC 25416中嘧啶的补救合成中具有活性。总体而言,洋葱伯克霍尔德菌ATCC 25416中的从头嘧啶合成在酶活性水平上受到调节,并且其嘧啶补救酶与在洋葱伯克霍尔德菌ATCC 17759中发现的酶不同。