Linked Life Data

10380113

Source:http://linkedlifedata.com/resource/pubmed/id/10380113

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-8-24
pubmed:databankReference
pubmed:abstractText
A serine protease of the silkworm, Bombyx mori, with an isoelectric point of pH 10-11 and a pH optimum for succinyl-Leu-Leu-Val-Tyr-MCA degrading activity of about 10, was found in a 0.33 M NaCl-eluted fraction obtained from cation-exchange chromatography of digestive juice. The activity of the enzyme was strongly inhibited by chymostatin and PMSF, indicating that the protease is a chymotrypsin-like serine protease. The N-terminal amino acid sequence of the protease was determined, and a full-length cDNA clone (0.92 kbp) which was isolated from a midgut cDNA library was sequenced. The cDNA encodes a pre-proenzyme of 284 amino acids with a pro-segment of 50 amino acids and mature protein of 234 amino acids. From its primary structure, the predicted molecular mass of the mature protein is 24.5 kDa. A sequence comparison of the Bombyx highly basic protease with other serine proteases revealed that this enzyme is a mammalian-type serine protease with a catalytic triad consisting of His45, Asp92 and Ser186. A large number of Arg residues are encoded by the cDNA which may be responsible for its stability and/or function in the alkaline condition, by remaining charged at high pH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0962-1075
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-304
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Cloning and sequence of a cDNA for a highly basic protease from the digestive juice of the silkworm, Bombyx mori.
pubmed:affiliation
Department of Applied Biology, Kyoto Institute of Technology, Japan. kotani@ipc.kit.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't