Reduction ofPDC1expression inS.cerevisiaewith xylose isomerase on xylose medium
β Scribed by Dong Min Kim; Seung-Hyun Choi; Byung Sam Ko; Gwon-Young Jeong; Han-Bit Jang; Jae-Gun Han; Kyung-Hwan Jeong; Hyeon-Yong Lee; Yonggwan Won; Il-Chul Kim
- Publisher
- Springer
- Year
- 2011
- Tongue
- English
- Weight
- 292 KB
- Volume
- 35
- Category
- Article
- ISSN
- 1615-7605
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The bacterial enzyme D-xylose isomerase (XI) catalyses the conversion of D-xylose to D-xylulose. Each subunit of the homotetrameric protein contains a bimetallic active centre requiring divalent metal ions such as Mg 2+ , Mn 2+ or Co 2+ for catalytic activity. We report here on XI in which the metal
The inactivation behavior of the xylose isomerase from Thermotoga neapolitana (TN5068 XI) was examined for both the soluble and immobilized enzyme. Polymolecular events were involved in the deactivation of the soluble enzyme. Inactivation was biphasic at 95Β°C, pH 7.0 and 7.9, the second phase was co