Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/42374
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- Title
- Activity-based identification of secreted serine proteases of the filamentous fungus, Ophiostoma
- Related
- Biotechnology letters, Vol. 29, No. 6, p.937-943
- DOI
- 10.1007/s10529-007-9333-6
- Publisher
- Springer
- Date
- 2007
- FoR/RFCD Code(s)
-
030401 Biologically Active Molecules
030503 Organic Chemical Synthesis
030599 Organic Chemistry not elsewhere classified
- Author/Creator
- Wu, Caiyan
- Author/Creator
- Xu, Qiang
- Author/Creator
- Liu, Fei
- Author/Creator
- Nevalainen, K. M. Helena
- Description
- A general activity probe was synthesized and applied to the supernatant of a filamentous fungus, Ophiostoma, culture to identify directly the secreted serine proteases by covalent enzyme labeling. The activity probe contained a chemically reactive group that reacted with, and thus covalently labeled, the serine residues of only active proteases and not heat-inactivated proteases. The activity probe also contained a fluorescent group that allowed for the subsequent visualization of the captured proteases in 1-D gels and their identification by N-terminal sequencing. This use of a chemical probe led to the rapid discovery of subtilisin-like serine protease of Ophiostoma. Two hypothetical proteins were also captured, with one being a probable endopeptidase K type of protease.
- Description
- 7 page(s)
- Subject Keyword
- 030401 Biologically Active Molecules
- Subject Keyword
- 030503 Organic Chemical Synthesis
- Subject Keyword
- 030599 Organic Chemistry not elsewhere classified
- Subject Keyword
- enzyme labeling
- Subject Keyword
- filamentous fungi
- Subject Keyword
- fluorescent activity probe
- Subject Keyword
- Ophiostoma
- Subject Keyword
- secreted proteases
- Resource Type
- journal article
- Organisation
- Macquarie University. Dept. of Chemistry and Biomolecular Sciences
- Identifier
- http://hdl.handle.net/1959.14/42374
- Identifier
- ISSN:1573-6776
- Identifier
- mq-rm-2007000776
- Language
- eng
- Reviewed
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