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.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Kang SH,Cho KK,Bok JD,Kim SC,Cho JS,Lee PC,Kang SK,Lee HG,Woo JH,Lee HJ,Lee SC,Choi YJdoi
10.1007/s00284-005-4467-zkeywords:
subject
Has Abstractpub_date
2006-04-01 00:00:00pages
243-8issue
4eissn
0343-8651issn
1432-0991journal_volume
52pub_type
杂志文章abstract::Tropical plants represent hotspots of endophytic fungal species diversity. Based on culture-dependent methods, we evaluated the endophytic fungal communities in leaves of three plant species found in the Brazilian Atlantic Rainforest: Begonia fischeri, Begonia olsoniae, and Begonia venosa. These species are found in t...
journal_title:Current microbiology
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journal_title:Current microbiology
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journal_title:Current microbiology
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journal_title:Current microbiology
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