Thermal denaturation of erythrocyte carbonic anhydrase.

Abstract

An experimental study on the thermal behaviour of erythrocyte carbonic anhydrase was carried out with the main aim to estimate the thermodynamic parameters that control the stability of the enzyme. The effects of thermal denaturation on the catalytic properties of the enzyme were also investigated. Below 60 degrees C the enzyme was found to be very stable, whereas between 60 and 65 degrees C a drastic decrease in the biological activity was observed. From the obtained results some considerations were made about the stabilization of the active form of the protein. Study holds ProTherm entries: 10121, 10122 Extra Details: carbonic anhydrase; thermal denaturation; conformational stability;,bovine erythrocytes

Submission Details

ID: 35X8xCNJ4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:39 p.m.

Version: 1

Publication Details
Lavecchia R;Zugaro M,FEBS Lett. (1991) Thermal denaturation of erythrocyte carbonic anhydrase. PMID:1959599
Additional Information

Study Summary

Number of data points 3
Proteins Carbonic anhydrase 2 ; Carbonic anhydrase 2
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: dG ; Experimental Assay: dCp ; Experimental Assay: Tm
Libraries Mutations for sequence A:MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK/K:QVQLVESGGGSVQAGGSLRLSCAASGYTVSTYCMGWFRQAPGKEREGVATILGGSTYYGDSVKGRFTISQDNAKNTVYLQMNSLKPEDTAIYYCAGSTVASTGWCSRLRPYDYHYRGQGTQVTVSS

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
1G6V 2000-11-08T00:00:00+0000 3.5 Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase
1V9E 2004-01-26T00:00:00+0000 1.95 Crystal Structure Analysis of Bovine Carbonic Anhydrase II
1V9I 2004-01-26T00:00:00+0000 2.95 Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II
4CNR 2014-01-24T00:00:00+0000 2.29 Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
4CNV 2014-01-25T00:00:00+0000 1.62 Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
4CNW 2014-01-25T00:00:00+0000 2.03 Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
4CNX 2014-01-25T00:00:00+0000 1.23 Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
5A25 2015-05-12T00:00:00+0000 1.9 Rational engineering of a mesophilic carbonic anhydrase to an extreme halotolerant biocatalyst
5EZT 2015-11-26T00:00:00+0000 1.54 Peracetylated Bovine Carbonic Anhydrase II
6SKS 2019-08-16T00:00:00+0000 1.75 Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH1)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Carbonic anhydrase 2 P86277 BIOR_THESB
92.3 Carbonic anhydrase 2 P00922 CAH2_SHEEP
100.0 Carbonic anhydrase 2 P00921 CAH2_BOVIN
100.0 A Carbonic anhydrase 2 P00918 CAH2_HUMAN