| Literature DB >> 16550460 |
Seung Ha Kang1, Kwang Keun Cho, Jin Duck Bok, Sung Chan Kim, Jaie Soon Cho, Peter Chang-Whan Lee, Sang Kee Kang, Hong Gu Lee, Jung Hee Woo, Hyun Jeong Lee, Sang Cheol Lee, Yun Jaie Choi.
Abstract
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 degrees C, respectively. Its specific activity on rho-nitrophenyl phosphatate was 70 U/mg at pH 5.5 and 40 degrees 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.Entities:
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Year: 2006 PMID: 16550460 DOI: 10.1007/s00284-005-4467-z
Source DB: PubMed Journal: Curr Microbiol ISSN: 0343-8651 Impact factor: 2.343