• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1249-1255
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• 2004

This study has developed Corynebacterium ammoniagenes (c. ammoniagenes) purine gene transcriptional reporters (purF-lacZ and purE-lacZ) that function in Escherichia coli (E. coli) DH5a. After transformation of a C. ammoniagenes gDNA library into E. coli cells harboring either purF-lacZ or purE-lacZ, C. ammoniagenes clones were obtained that repress purF-lacZ and purE-lacZ gene expression. The potential purE and purF regulatory genes are homologous to the genes encoding transcription regulators, the regulatory subunit of RNA polymerase, and genes for purine nucleotide biosynthesis of various bacteria. The C. ammoniagenes purE-lacZ and purF-lacZ reporters were repressed by adenine and guanine within E. coli, indicating similarity in the regulatory mechanism of purine biosynthesis in C. ammoniagenes and E. coli. Gene regulation of pur-lacZ by adenine and guanine was partly abolished in cells expressing potential purine regulatory genes, indicating functionality of the purine gene regulators in repression of purE-lacZ and purF-lacZ. The purE-lacZ and purF-lacZ reporters can be used for the screening of genes involved in the regulation of the de novo synthesis of the purine nucleotides.

• 대한약학회:학술대회논문집
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• 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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• pp.181.2-181.2
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• 2003

Inosine monophosphate dehydrogenase(IMPDH) catalyzes the $NAD^+$-dependent oxidation of IMP to XMP, the rate limiting step in the de novo biosynthesis of guanine nucleotide. Its critical role at the metabolic branch point in purine nucleotide biosynthesis makes it a useful target in the development of drugs for antiviral and anticancer chemotherapy and in immunosupressant area. Several compound with antiviral activity have been found to be inhibitors of IMPDH. For example, ribavirin, a competitive inhibitor of IMPDH, has broad spectrum antiviral activities against DNA and RNA viruses. (omitted)