Document Detail


Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori. Purification, characterization, and cDNA cloning.
MedLine Citation:
PMID:  10066809     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Prophenoloxidase-activating enzyme (PPAE) was purified to homogeneity as judged by SDS-polyacrylamide gel electrophoresis from larval cuticles of the silkworm, Bombyx mori. The purified PPAE preparation was shown to be a mixture of the isozymes of PPAE (PPAE-I and PPAE-II), which were eluted at different retention times in reversed-phase high performance liquid chromatography. PPAE-I and PPAE-II seemed to be post translationally modified isozymes and/or allelic variants. Both PPAE isozymes were proteins composed of two polypeptides (heavy and light chains) that are linked by disulfide linkage(s) and glycosylated serine proteases. The results of cDNA cloning, peptide mapping, and amino acid sequencing of PPAE revealed that PPAE is synthesized as prepro-PPAE with 441 amino acid residues and is activated from pro-PPAE by cleavage of a peptide bond between Lys152 and Ile153. The homology search showed 36.9% identity of PPAE to easter, which is a serine protease involved in dorso-ventral pattern formation in the Drosophila embryo, and indicated the presence of two consecutive clip-like domains in the light chain. A single copy of the PPAE gene was suggested to be present in the silkworm genome. In the fifth instar larvae, PPAE transcripts were detected in the integument, hemocytes, and salivary glands but not in the fat body or mid gut. A polypeptide cross-reactive to mono-specific anti-PPAE/IgG was transiently detected in the extract of eggs between 1 and 3 h after they were laid.
Authors:
D Satoh; A Horii; M Ochiai; M Ashida
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  274     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1999 Mar 
Date Detail:
Created Date:  1999-04-13     Completed Date:  1999-04-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7441-53     Citation Subset:  IM    
Affiliation:
Biochemistry Laboratory, The Institute of Low Temperature Science, Hokkaido University, Sapporo, 060-0189 Japan.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AB009670
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / analysis
Animals
Blotting, Southern
Bombyx / enzymology*
Carbohydrates / analysis
Catechol Oxidase / metabolism*
Chromatography, Ion Exchange / methods
Cloning, Molecular
Cross Reactions
DNA, Complementary
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Enzyme Precursors / chemistry,  genetics,  isolation & purification*,  metabolism*
Hemocytes / enzymology
Isoelectric Point
Molecular Sequence Data
Molecular Weight
Peptide Hydrolases / chemistry,  genetics,  isolation & purification*
Sequence Homology, Amino Acid
Serine Endopeptidases*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Carbohydrates; 0/DNA, Complementary; 0/Enzyme Precursors; EC 1.10.3.-/pro-phenoloxidase; EC 1.10.3.1/Catechol Oxidase; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.-/prephenoloxidase-activating enzyme

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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