Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis.
The glmU gene product of Escherichia coli was recently identified as the N-acetylglucosamine-1-phosphate uridyltransferase activity which catalyzes the formation of UDP-N-acetylglucosamine, an essential precursor for cell wall peptidoglycan and lipopolysaccharide biosyntheses (D. Mengin-Lecreulx and...
保存先:
| 出版年: | J Bacteriol |
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| 主要な著者: | , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1994
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC196783/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8083170/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.176.18.5788-5795.1994 |
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