Linked Life Data

7654769

Source:http://linkedlifedata.com/resource/pubmed/id/7654769

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-10-3
pubmed:abstractText
The extracellular serine proteinase secreted by Ophiostoma piceae was degraded by autoproteolysis under certain conditions. At elevated temperatures the mature protein of 33 kDa was rapidly degraded without any accumulation of protein breakdown products. Glycerol, calcium ions and ammonium sulfate raised the heat stability of the enzyme, increasing its half-life at 45 degrees C from 1.9 min to 9.4 min, 40.4 min and 2 h, respectively. Thermal unfolding of the proteinase also occurred at higher temperatures in the presence of calcium ions and ammonium sulfate. Under conditions of heating, altered pH or partial depletion of protein-bound ions by EDTA, the structure of the proteinase was more susceptible to proteolysis. The major hydrolytic fragments of 19 kDa and 14 kDa, had N-terminal sequences of Ala1-Tyr2-Thr3-Thr4-Gln5-Thr6-Gly7-Ala8-Pro9-and Ser170-Glu171-Pro172-Se173-Val174-X-Thr 176-Val177-Gly178-Ala179-, respectively. Since the former sequence was identical to the N-terminus of the native protein, the major autoproteolytic cleavage site for a class II subtilase appeared to be the N-side of Ser170 using numbering based on the sequence of proteinase K. The secondary structure of the proteinase from O. piceae was similar to that of proteinase K based on circular dichroic spectra in the far ultraviolet region. This cleavage site was in a similar region to that identified for class I subtilases, which was located in an outer exposed loop of the tertiary structure of subtilisin-like serine proteinases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
1245
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
76-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Factors affecting autolysis of a subtilisin-like serine proteinase secreted by Ophiostoma piceae and identification of the cleavage site.
pubmed:affiliation
Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancoucer, Canada.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't