The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation.
The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation.
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枯草芽孢杆菌 Gne (GneA、GalE) 蛋白可以催化 UDP-葡萄糖以及 UDP-N-乙酰氨基葡萄糖 4-差向异构化。
DOI：
10.1016/s0378-1119(03)00793-5
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发表时间：
2003
期刊：
影响因子：
3.5
通讯作者：
V. Lazarevic
中科院分区：
文献类型：
--
作者：
B. Soldo;C. Scotti;D. Karamata;V. Lazarevic
影响尿苷二磷酸(UDP)- n -乙酰氨基葡萄糖（GlcNAc） 4-外亚胺酶（EC 5.1.3.7）活性的枯草芽孢杆菌基因突变，被证实与UDP-葡萄糖（Glc） 4-外亚胺酶（EC 5.1.3.2）的结构基因galE相关。这种基因证据表明，同一酶可以催化己糖及其n -乙酰化形式的外聚体化，并通过纯化酶的体外测定得到证实。在枯草芽孢杆菌中，Gne （GneA, GalE）似乎参与了两种不同的基本功能，即在特定生长条件下的细胞解毒和阴离子细胞壁聚合物的生物合成。我们讨论的证据表明，这种酶能够利用双方的udp -己糖和udp - n -乙酰己糖胺存在于其他生物体。
Mutations in the Bacillus subtilis gene that affect the activity of the uridine diphosphate (UDP)-N-acetylglucosamine (GlcNAc) 4-epimerase (EC 5.1.3.7) were shown to map to galE, the structural gene of the UDP-glucose (Glc) 4-epimerase (EC 5.1.3.2). This genetic evidence that the same enzyme can catalyse the epimerisation of hexoses as well as of their N-acetylated forms is confirmed by in vitro assays with purified enzyme. It appears that in B. subtilis, Gne (GneA, GalE) is involved in two distinct and essential functions, i.e., cell detoxification under certain growth conditions and the biosynthesis of anionic cell wall polymers. We discuss the evidence that such enzymes capable of utilizing both UDP-hexoses and UDP-N-acetylhexosamines are present in other organisms.
影响因子：
64.8
作者：
Kunst, F;Ogasawara, N;Danchin, A
通讯作者：
Danchin, A