Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase.
Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase.
复制标题
尿苷二磷酸-N-乙酰胞壁酸的生物合成。
DOI：
--
复制
发表时间：
1970
影响因子：
4.8
通讯作者：
R. Anwar
中科院分区：
文献类型：
--
作者：
A. Taku;K. G. Gunetileke;R. Anwar
尿苷-5 ′-二磷酸-N-乙酰基-2-氨基-2-脱氧-3-O-乳酰葡萄糖：NADP-氧化还原酶，一种催化还原UDP-GlcNAc-烯醇丙酮酸形成尿苷-5 ′-二磷酸-N-乙酰胞壁酸的酶，从阴沟肠杆菌NRC 492中纯化了151倍。反应的最适pH范围为8.1 ~ 8.5。UDP-GlcNAc-烯醇丙酮酸的Km为4.0 x 10-5 m，NADPH的Km为4.9 x 10-5 m。现有的数据表明，该酶需要一个硫醇基团（或基团）的活性，并含有FAD作为辅基。
Abstract Uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase, an enzyme which catalyzes the reduction of UDP-GlcNAc-enolpyruvate to form uridine-5'-diphospho-N-acetylmuramic acid, was purified 151-fold from Enterobacter cloacae NRC 492. The optimum pH range for the reaction was from 8.1 to 8.5. The Km for UDP-GlcNAc-enolpyruvate was 4.0 x 10-5 m and that for NADPH was 4.9 x 10-5 m. The available data suggest that the enzyme requires a thiol group (or groups) for its activity and contains FAD as the prosthetic group.