Factors effecting the thermostability of cysteine proteinases from Carica papaya.
Abstract
Thermal denaturation of four Carica papaya cysteine proteinases (papain, chymopapain, papaya proteinases 3 and 4) was studied as a function of pH using high-sensitivity differential scanning calorimetry. The ratios of calorimetric enthalpy to Van't Hoff enthalpy suggest that, for all these proteins, denaturation occurs as a non two state process, via an intermediate structure. Differences in the thermal stabilities of the proteinases; chymopapain > papaya proteinase 3 > papain > papaya proteinase 4, were correlated to their amino acid sequence to explain the observations in terms of mobility and specific residue mutation. Three-dimensional structures of papain and papaya proteinase 3 were similarly used to illustrate the influence of atomic mobility on stability. Study holds ProTherm entries: 7577, 7578, 7579, 7580, 7581, 7582, 7583, 7584, 7585, 7586, 7587, 7588, 7589, 7590, 7591, 7592, 7593, 7594, 7595, 7596 Extra Details:
Submission Details
ID: MWVJ5Cea3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:34 p.m.
Version: 1
Publication Details
Sumner IG;Harris GW;Taylor MA;Pickersgill RW;Owen AJ;Goodenough PW,Eur. J. Biochem. (1993) Factors effecting the thermostability of cysteine proteinases from Carica papaya. PMID:8508784Additional Information
Study Summary
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
|---|
Data Distribution
Studies with similar sequences (approximate matches)
Correlation with other assays (exact sequence matches)
Relevant PDB Entries
| Structure ID | Release Date | Resolution | Structure Title |
|---|---|---|---|
| 1YAL | 1996-06-20T00:00:00+0000 | 1.7 | CARICA PAPAYA CHYMOPAPAIN AT 1.7 ANGSTROMS RESOLUTION |
| 1BP4 | 1998-08-12T00:00:00+0000 | 2.2 | USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED DESIGN OF CATHEPSIN K INHIBITORS. CRYSTAL STRUCTURES OF TWO PAPAIN INHIBITOR COMPLEXES DEMONSTRATE BINDING TO S'-SUBSITES. |
| 1BQI | 1998-08-16T00:00:00+0000 | 2.5 | USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED DESIGN OF CATHEPSIN K INHIBITORS. CRYSTAL STRUCTURES OF TWO PAPAIN INHIBITOR COMPLEXES DEMONSTRATE BINDING TO S'-SUBSITES. |
| 1CVZ | 1999-08-24T00:00:00+0000 | 1.7 | CRYSTAL STRUCTURE ANALYSIS OF PAPAIN WITH CLIK148(CATHEPSIN L SPECIFIC INHIBITOR) |
| 1KHP | 2001-11-30T00:00:00+0000 | 2.0 | Monoclinic form of papain/ZLFG-DAM covalent complex |
| 1KHQ | 2001-11-30T00:00:00+0000 | 1.6 | ORTHORHOMBIC FORM OF PAPAIN/ZLFG-DAM COVALENT COMPLEX |
| 1PAD | 1976-11-01T00:00:00+0000 | 2.8 | Binding of chloromethyl ketone substrate analogues to crystalline papain |
| 1PE6 | 1991-05-14T00:00:00+0000 | 2.1 | REFINED X-RAY STRUCTURE OF PAPAIN(DOT)E-64-C COMPLEX AT 2.1-ANGSTROMS RESOLUTION |
| 1PIP | 1992-10-03T00:00:00+0000 | 1.7 | CRYSTAL STRUCTURE OF PAPAIN-SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE COMPLEX AT 1.7 ANGSTROMS RESOLUTION: NONCOVALENT BINDING MODE OF A COMMON SEQUENCE OF ENDOGENOUS THIOL PROTEASE INHIBITORS |
| 1POP | 1993-06-24T00:00:00+0000 | 2.1 | X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A PAPAIN-LEUPEPTIN COMPLEX |