Search Reference

3.4.22.25

Three-dimensional structure and thiol reactivity characteristics of chymopapain M (papaya proteinase IV)

Biochem. Soc. Trans.

18

934-935

1990

3.4.22.25

The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin

Biochem. J.

306

39-46

1995

3.4.22.25

The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases

FEBS Lett.

434

401-405

1998

3.4.22.25

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

Biochem. J.

300

805-820

1994

3.4.22.25

Structural characterization of the papaya cysteine proteinases at low pH

Biochem. Biophys. Res. Commun.

341

620-626

2006

3.4.22.25

Solid-to-solid peptide synthesis by glycyl endopeptidase

Enzyme Microb. Technol.

40

954-960

2007

-

3.4.22.25

Selective cleavage of glycyl bonds by papaya proteinase IV

FEBS Lett.

260

195-197

1990

3.4.22.25

Papaya proteinase IV amino acid sequence

FEBS Lett.

258

109-112

1989

3.4.22.25

Kinetic constants for the hydrolysis of aggrecan by the papaya proteinases and their relevance for chemonucleolysis

Arch. Biochem. Biophys.

320

375-379

1995

3.4.22.25

Isolation of highly active papaya peptidases A and B from commercial chymopapain

Biochim. Biophys. Acta

658

262-269

1981