Linked Life Data

11179955

Source:http://linkedlifedata.com/resource/pubmed/id/11179955

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-2-22
pubmed:databankReference
pubmed:abstractText
The prophenoloxidase activating enzyme (ppA), a serine proteinase catalyzing the conversion of prophenoloxidase to an active phenoloxidase, has a molecular mass of about 36 kDa in its active form. This protein was cloned from a blood cell cDNA library and its corresponding cDNA of 1736 base pairs encodes a zymogenic protein (proppA) of 468 amino acids. An antibody raised against a synthetic peptide derived from a region of the cDNA sequence could efficiently inhibit the beta-1,3-glucan triggered activation of prophenoloxidase in vitro. The C-terminal half of the proppA is composed of a typical serine proteinase domain, with a sequence similar to other invertebrate and vertebrate serine proteinases. The N-terminal half contains a cationic glycine-rich domain, a cationic proline-rich domain and a clip-domain, in which the disulfide-bonding pattern is likely to be identical to those of the horseshoe crab big defensin and mammalian beta-defensins. Antibodies made against both the C- and the N-terminal halves recognize two proppAs under reducing conditions. However, under nonreducing conditions only the anti-C antibody recognized the two proppAs, which suggests that a conformational change takes place upon reduction that allows the anti-N to react with the N-terminal half of proppA. The recombinant clip-domain in crayfish proppA was overexpressed in Escherichia coli and the resulting peptide exhibited antibacterial activity against Gram-positive bacterial strains such as Micrococcus luteus Ml11 and Bacillus megaterium Bm11 with 50% growth inhibitory concentrations of 1.43 microM and 17.9 microM, respectively. These results suggest that the clip-domains in proppAs may function as antibacterial peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
895-902
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:11179955-Amino Acid Sequence, pubmed-meshheading:11179955-Animals, pubmed-meshheading:11179955-Astacoidea, pubmed-meshheading:11179955-Base Sequence, pubmed-meshheading:11179955-Cloning, Molecular, pubmed-meshheading:11179955-Defensins, pubmed-meshheading:11179955-Enzyme Activation, pubmed-meshheading:11179955-Enzyme Precursors, pubmed-meshheading:11179955-Gene Expression, pubmed-meshheading:11179955-Gram-Positive Bacteria, pubmed-meshheading:11179955-Insect Proteins, pubmed-meshheading:11179955-Molecular Sequence Data, pubmed-meshheading:11179955-Peptide Hydrolases, pubmed-meshheading:11179955-Peptides, pubmed-meshheading:11179955-Protein Structure, Tertiary, pubmed-meshheading:11179955-RNA, Messenger, pubmed-meshheading:11179955-Sequence Homology, Amino Acid, pubmed-meshheading:11179955-Serine Endopeptidases
pubmed:year
2001
pubmed:articleTitle
Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus.
pubmed:affiliation
Department of Comparative Physiology, Evolutionary Biology Centre, Uppsala University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't