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:8508784
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
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

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Papain P00784 PAPA1_CARPA
100.0 Chymopapain P14080 PAPA2_CARPA
90.7 Chymopapain P32956 CYSP3_VASCU