In a recent study we showed that two proteinases (CMS2MS2 and CMS2MS3) from Carica candamarcensis enhance mammalian cell proliferation. The aim of the present study is the determination of the primary structure of CMS2MS2 and prediction of its three-dimensional structure. The protein contains 214 residues, including the catalytic triad composed of Cys(25), His(159), and Asn(175). A phylogenetic tree analysis demonstrated that CMS2MS2 ranks closer to chymopapain than to papain. The overall predicted three-dimensional structure is similar to proteinases from the papain family. These results suggest that minor structural differences within CMS2MS2 must account for its proliferative action.
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X-ray crystal structure of CMS1MS2: a high proteolytic activity cysteine proteinase from Carica candamarcensis.
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Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos 6627, Belo Horizonte, MG, 31270-901, Brazil.
CMS1MS2 (CC-Ib) from Carica candamarcensis (Vasconcellea cundinamarcensis) is a cysteine proteinase found as a single polypeptide containing 213 residues of 22,991 Da. The enzyme was purified by three chromatographic steps, two of them involving cationic exchange. Crystals of CMS1MS2 complexed with E-64 were obtained by the hanging drop vapor-diffusion method at 291 K using ammonium sulfate and polyethylene glycol 4000/8000 as precipitant.
View Article and Find Full Text PDFMolecular cloning of a mitogenic proteinase from Carica candamarcensis: its potential use in wound healing.
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November 2011
Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, UFMG 31270-901, Belo Horizonte, MG, Brazil.
Cysteine proteinases from the Caricaceae belong to the C1 family of the CA clan and display papain-like structured, the archetype enzyme for this group of proteins. Carica candamarcensis, also named Vasconcellea cundinamarcensis, a member of Caricaceae family common to many areas in South America, contains cysteine proteinases with proteolytic activity five to eight-fold higher than those from latex of Carica papaya. The cysteine protease CMS2MS2 from C.
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Departamento de Bioquímica, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
The lattices of Carica candamarcensis and Carica papaya, members of the Caricaceae family, contain isoforms of cysteine proteinases that help protect these plants against injury. In a prior study, we fractionated 14 discrete proteinaceous components from C. candamarcensis, two of them displaying mitogenic activity in mammalian cells.
View Article and Find Full Text PDFThe structure of CMS2MS2, a mitogenic protein isolated from Carica candamarcensis.
Biol Chem
August 2007
Departamentos de Bioquímica e Imunologia, Farmacologia, Instituto de Ciências Biológicas, Universidade Federal Minas Gerais, Avenida Antônio Carlos 6627, 31270-901 Belo Horizonte, MG, Brazil.
In a recent study we showed that two proteinases (CMS2MS2 and CMS2MS3) from Carica candamarcensis enhance mammalian cell proliferation. The aim of the present study is the determination of the primary structure of CMS2MS2 and prediction of its three-dimensional structure. The protein contains 214 residues, including the catalytic triad composed of Cys(25), His(159), and Asn(175).
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