Literature DB >> 518921

N-Terminal homology in three cysteinyl proteases from Papaya latex.

K R Lynn, M Yaguchi.   

Abstract

Sequences to residue 17 have been determined for the three Papaya cysteinyl proteases, chymopapain and papaya peptidase A and B. Extensive homologies were found for these three enzymes and with papain and bromelain. These results suggest that the five sulphydryl enzymes discussed derive from a common ancestral gene.

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Year:  1979        PMID: 518921     DOI: 10.1016/0005-2795(79)90257-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Structural similarity of chymopapain forms as indicated by circular dichroism.

Authors:  S Solis-Mendiola; R Zubillaga-Luna; A Rojo-Dominguez; A Hernandez-Arana
Journal:  Biochem J       Date:  1989-01-01       Impact factor: 3.857

2.  Problems of classification of papaya latex proteinases.

Authors:  L Polgár
Journal:  Biochem J       Date:  1984-07-15       Impact factor: 3.857

3.  Funastrain c II: a cysteine endopeptidase purified from the latex of Funastrum clausum.

Authors:  Susana R Morcelle; Sebastián A Trejo; Francesc Canals; Francesc X Avilés; Nora S Priolo
Journal:  Protein J       Date:  2004-04       Impact factor: 2.371

4.  Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.

Authors:  M P Thomas; C M Topham; D Kowlessur; G W Mellor; E W Thomas; D Whitford; K Brocklehurst
Journal:  Biochem J       Date:  1994-06-15       Impact factor: 3.857

  4 in total

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