Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain.


Abstract

High-sensitivity differential scanning calorimetry has been applied to the study of porcine pancreatic carboxypeptidase B, the proenzyme and its 81-residue activation domain. The thermal study has been carried out over a range of scan rates, ionic strengths and pH values. The thermal unfolding of the isolated activation domain has been found to be reversible and corresponds to that of a typical compact globular structure, with melting temperatures higher than those of the enzyme and proenzyme. Both proteins, on the other hand, undergo an irreversible, highly scan-rate-dependent thermal denaturation under all the experimental conditions investigated. The denaturation of the enzyme at pH 7.5 and the proenzyme at pH 7.5 and 9.0 follows the two-state irreversible model [Sánchez-Ruiz, J.M., López-Lacomba, J.L., Cortijo, M. & Mateo, P.L. (1988) Biochemistry 27, 1648-1652]. Thus the kinetic constants and activation parameters of the denaturation process could be obtained and compared to those for other proteins, particularly those of the closely related carboxypeptidase A system. Study holds ProTherm entries: 7515, 7516, 7517, 7518, 7519, 7520, 7521, 7522, 7523, 7524, 7525, 7526, 7527, 7528, 7529, 7530, 7531, 7532, 7533, 7534, 7535, 7536, 7537, 7538, 7539, 7540, 7541, 7542, 7543, 7544, 7545, 7546 Extra Details: activation domain; compact globular structure;,scan-rate-dependent; kinetic constants

Submission Details

ID: THQRMZSm3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Conejero-Lara F;Sánchez-Ruiz JM;Mateo PL;Burgos FJ;Vendrell J;Avilés FX,Eur. J. Biochem. (1991) Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain. PMID:1915340
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
1NSA 1997-07-25T00:00:00+0000 2.3 THREE-DIMENSIONAL STRUCTURE OF PORCINE PROCARBOXYPEPTIDASE B: A STRUCTURAL BASIS OF ITS INACTIVITY
1PBA 1991-11-18T00:00:00+0000 0 THE NMR STRUCTURE OF THE ACTIVATION DOMAIN ISOLATED FROM PORCINE PROCARBOXYPEPTIDASE B
1Z5R 2005-03-18T00:00:00+0000 1.4 Crystal Structure of Activated Porcine Pancreatic Carboxypeptidase B
1ZG7 2005-04-20T00:00:00+0000 1.75 Crystal Structure of 2-(5-{[amino(imino)methyl]amino}-2-chlorophenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B
1ZG8 2005-04-20T00:00:00+0000 2.0 Crystal Structure of (R)-2-(3-{[amino(imino)methyl]amino}phenyl)-3-sulfanylpropanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B
1ZG9 2005-04-20T00:00:00+0000 2.0 Crystal Structure of 5-{[amino(imino)methyl]amino}-2-(sulfanylmethyl)pentanoic acid Bound to Activated Porcine Pancreatic Carboxypeptidase B
2JEW 2007-01-24T00:00:00+0000 1.4 Crystal structure of ((2S)-5-amino-2-((1-n-propyl-1H-imidazol-4-yl) methyl)pentanoic acid) UK396,082 a TAFIa inhibitor, Bound to Activated Porcine Pancreatic carboxypeptidaseB
2PIY 2007-04-15T00:00:00+0000 1.43 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B (S)-2-(3-Aminomethyl-phenyl)-3-{hydroxy-[(R)-2-methyl-1-(3-phenyl-propane-1-sulfonylamino)-propyl]-phosphinoyl}-propionic acid {ZK 528} COMPLEX
2PIZ 2007-04-15T00:00:00+0000 1.6 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B 2-(3-Guanidino-phenyl)-3-[hydroxy-(3-phenyl-propyl)-phosphinoyl]-propionic acid COMPLEX
2PJ0 2007-04-15T00:00:00+0000 1.65 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B [((R)-1-Benzyloxycarbonylamino-2-methyl-propyl)-hydroxy-phosphinoyloxy]-(3-guanidino-phenyl)-acetic acid COMPLEX

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Carboxypeptidase B P09955 CBPB1_PIG