Isolation, Characterization, and Structure of Procathepsin E and Cathepsin E from the Gastric Mucosa of Guinea Pig

A Caenorhabditis elegans gene (asp-1) and cDNA that encode a homologue of cathepsin D aspartic protease were cloned and characterized. The asp-1 mRNA is transcribed from a single exon, and it begins with the SL1 trans-splice leader sequence. The protein (ASP-1) is expressed as a 396-amino acid, 42.7-kDa pre-pro-peptide that is post-translationally processed into a ϳ40-kDa lysosomal protein. ASP-1 shares ϳ60% sequence identity with the aspartic protease precursor from the nematode Strongyloides stercoralis. The amino acid sequences adjacent to the two active site aspartic acid residues in ASP-1 are 100% identical to those in other eukaryotic aspartic proteases. In addition, ASP-1 contains conserved, potential disulfide bond-forming cysteine residues and N-glycosylation sites. The asp-1 gene is exclusively transcribed in the intestinal cells, with the highest levels of expression observed at late embryonic and early larval stages of development. asp-1 transcription is not observed in adult nematodes or mature larvae. Furthermore, transcription predominantly occurs in eight anterior cells of the intestine (int6-int8). Analyses of ASP-1 nucleotide and amino acid sequences revealed the presence of five additional C. elegans aspartic proteases.

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Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T<sub>1</sub> to carboxyl peptidases

Takahashi

2013

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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A group of enzymes, mostly hydrolases or certain transferases, utilize one or a few side-chain carboxyl groups of Asp and/or Glu as part of the catalytic machinery at their active sites. This review follows mainly the trail of studies performed by the author and his colleagues on the structure and function of such enzymes, starting from ribonuclease T1, then extending to three major types of carboxyl peptidases including aspartic peptidases, glutamic peptidases and serine-carboxyl peptidases.

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Isolation, Characterization, and Structure of Procathepsin E and Cathepsin E from the Gastric Mucosa of Guinea Pig

Cited by 3 publications

References 33 publications

Cathepsin E

Cathepsin E

Aspartic Proteases from the Nematode Caenorhabditis elegans

Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T<sub>1</sub> to carboxyl peptidases

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