Literature DB >> 10607668

Novel ways to prevent proteolysis - prophytepsin and proplasmepsin II.

N K Bernstein1, M N James.   

Abstract

The recently determined crystal structures of two aspartic proteinase zymogens, prophytepsin from barley and proplasmepsin II from the malarial parasite Plasmodium falciparum, have provided new insights into zymogen inactivation. Prophytepsin shows a variation of the mechanism of inhibition used by the well-known gastric aspartic proteinase zymogens, whereas proplasmepsin II uses a completely new mode of inactivation.

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Year:  1999        PMID： 10607668     DOI： 10.1016/s0959-440x(99)00030-5

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  4 in total

1.  Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase.

Authors:  Kenneth G Payie; Takuji Tanaka; Susannah Gal; Rickey Y Yada
Journal:  Biochem J       Date:  2003-06-15       Impact factor: 3.857

2.  Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins.

Authors:  Rosario Recacha; Kristaps Jaudzems; Inara Akopjana; Aigars Jirgensons; Kaspars Tars
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2016-08-09       Impact factor: 1.056

3.  Site-directed mutagenesis and structural studies suggest that the germination protease, GPR, in spores of Bacillus species is an atypical aspartic acid protease.

Authors:  Thomas M Carroll; Peter Setlow
Journal:  J Bacteriol       Date:  2005-10       Impact factor: 3.490

4.  Activation mechanism of plasmepsins, pepsin-like aspartic proteases from Plasmodium, follows a unique trans-activation pathway.

Authors:  Ishan Rathore; Vandana Mishra; Chandan Patel; Huogen Xiao; Alla Gustchina; Alexander Wlodawer; Rickey Y Yada; Prasenjit Bhaumik
Journal:  FEBS J       Date:  2020-05-26       Impact factor: 5.622
  4 in total

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