| Autor: |
OKUYAMA, Kiyoshi, HAMAMOTO, Tomoki, ISHIGE, Kazuya, TAKENOUCHI, Kenji, NOGUCHI, Toshitada |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2000, Vol. 64 Issue: 2 p386-392, 7p |
| Abstrakt: |
Uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc) has been synthesized by a yeast-based method from 5′-UMP and glucosamine, in which yeast cells catalyze the conversion of 5′-UMP to 5′-UTP and provide enzymes involved in UDP-GlcNAc synthesis using 5′-UTP and glucosamine as substrates. However, this conventional method is not suitable for practical production of UDP-GlcNAc because of the low yield of the product. We found that the yqgRgene product of Bacillus subtilis, which has been identified as a glucokinase, can catalyze the phosphorylation of N-acetylglucosamine (GlcNAc) to give GlcNAc-6-phosphate, an intermediate of UDP-GlcNAc biosynthesis. The addition of the yqgRgene product to the yeast-based reaction system enabled us to synthesize UDP-GlcNAc using GlcNAc in place of glucosamine. The addition of two enzymes, GlcNAc-phosphate mutase and UDP-GlcNAc pyrophosphorylase, increased the yield of UDP-GlcNAc. Using this novel method, UDP-GlcNAc was produced at an amount of 78 mMfrom 100 mM5′-UMP and 100 mMGlcNAc. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
