| Autor: |
Seung Ha Kang, Kwang Keun Cho, Jin Duck Bok, Sung Chan Kim, Jaie Soon Cho, Chang-whan Lee, Peter, Sang Kee Kang, Hong Gu Lee, Jung Hee Woo, Hyun Jeong Lee, Sang Cheol Lee, Yun Jaei Choi |
| Předmět: |
|
| Zdroj: |
Current Microbiology; Apr2006, Vol. 52 Issue 4, p243-248, 6p, 2 Diagrams, 1 Chart, 6 Graphs |
| Abstrakt: |
A gene, phoI, coding for a phosphatase from Enterobacter sp. 4 was cloned in Escherichia coli and sequenced. Analysis of the sequence revealed one open reading frame (ORF) that encodes a 269–amino acid protein with a calculated molecular mass of 29 kDa. PhoI belongs to family B acid phosphatase and exhibits 49.4% identity and 62.4% homology to the hel gene from Heamophilus influenzae, which encoded an outer membrane protein (P4). The optimum pH and temperature for phosphatase activity were pH 5.5 and 40°C, respectively. Its specific activity on ρ-nitrophenyl phosphatate was 70 U/mg at pH 5.5 and 40°C. Enzyme activity was inhibited by Al3+, EDTA, and DTT, but fivefold activated by Cu2+ ion (350 U/mg). PhoI showed a strong synergistic effect when used with a purified E. coli phytase, AppA, to estimate combination effects. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Full text from SpringerLink