Literature DB >> 8163018

Multiple functions of pro-parts of aspartic proteinase zymogens.

G Koelsch1, M Mares, P Metcalf, M Fusek.   

Abstract

The importance of aspartic proteinases in human pathophysiology continues to initiate extensive research. With burgeoning information on their biological functions and structures, the traditional view of the role of activation peptides of aspartic proteinases solely as inhibitors of the active site is changing. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. Consequently, the primary structures of pro-parts reflect these functions. We discuss guidelines for formation of hypotheses derived from comparing the physiological function of aspartic proteinases and sequences of their pro-parts.

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Year:  1994        PMID: 8163018     DOI: 10.1016/0014-5793(94)80596-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  19 in total

1.  Identification of furin pro-region determinants involved in folding and activation.

Authors:  Lyne Bissonnette; Gabriel Charest; Jean-Michel Longpré; Pierre Lavigne; Richard Leduc
Journal:  Biochem J       Date:  2004-05-01       Impact factor: 3.857

2.  Post-translational regulation of CND41 protease activity in senescent tobacco leaves.

Authors:  Yusuke Kato; Yumiko Yamamoto; Shinya Murakami; Fumihiko Sato
Journal:  Planta       Date:  2005-11-04       Impact factor: 4.116

3.  Molecular characterization of cycloinulooligosaccharide fructanotransferase from Bacillus macerans.

Authors:  H Y Kim; Y J Choi
Journal:  Appl Environ Microbiol       Date:  2001-02       Impact factor: 4.792

4.  Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).

Authors:  Q N Cao; M Stubbs; K Q Ngo; M Ward; A Cunningham; E F Pai; G C Tu; T Hofmann
Journal:  Protein Sci       Date:  2000-05       Impact factor: 6.725

5.  Chlapsin, a chloroplastidial aspartic proteinase from the green algae Chlamydomonas reinhardtii.

Authors:  Carla Malaquias Almeida; Cláudia Pereira; Diana Soares da Costa; Susana Pereira; José Pissarra; Isaura Simões; Carlos Faro
Journal:  Planta       Date:  2012-02-19       Impact factor: 4.116

6.  Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B.

Authors:  Valérie Laurent-Matha; Danielle Derocq; Christine Prébois; Nobuhiko Katunuma; Emmanuelle Liaudet-Coopman
Journal:  J Biochem       Date:  2006-03       Impact factor: 3.387

7.  Structural insights into the activation and inhibition of histo-aspartic protease from Plasmodium falciparum.

Authors:  Prasenjit Bhaumik; Huogen Xiao; Koushi Hidaka; Alla Gustchina; Yoshiaki Kiso; Rickey Y Yada; Alexander Wlodawer
Journal:  Biochemistry       Date:  2011-09-26       Impact factor: 3.162

8.  The DNA-binding protease, CND41, and the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in senescent leaves of tobacco.

Authors:  Yusuke Kato; Shinya Murakami; Yumiko Yamamoto; Hiroshi Chatani; Yoshihiko Kondo; Takeshi Nakano; Akiho Yokota; Fumihiko Sato
Journal:  Planta       Date:  2004-07-14       Impact factor: 4.116

Review 9.  Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin.

Authors:  C Richter; T Tanaka; R Y Yada
Journal:  Biochem J       Date:  1998-11-01       Impact factor: 3.857

10.  Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway.

Authors:  Patrícia Duarte; José Pissarra; Ian Moore
Journal:  Planta       Date:  2008-02-14       Impact factor: 4.116

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