Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein

European Journal of Biochemistry

Volumn 267, Issue 19, 2000, Pages 5908-5915

  Elleby, Björn ^a   Sjöblom, Björn ^a   Tu, Chingkuang ^b   Silverman, David N ^b   Lindskog, Sven ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b UNIVERSITY OF FLORIDA   (United States)

Author keywords

Carbonic anhydrase related protein; Catalytic activity; Kinetics; Mutagenesis

Indexed keywords

ARGININE; CARBONATE DEHYDRATASE; HISTIDINE; ZINC;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; ESCHERICHIA COLI; KINETICS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANIMAL; BINDING SITES; CARBON DIOXIDE; CATALYSIS; CIRCULAR DICHROISM; COMPARATIVE STUDY; HYDROGEN-ION CONCENTRATION; KINETICS; MICE; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT FUSION PROTEINS; SUPPORT, NON-U.S. GOV'T; ZINC;

EID: 0033802752     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01644.x     Document Type: Article

References (30)

1. Functional diversity, conservation, and convergence in the evolution of α-, β-, and γ-carbonic anhydrase gene families
2. Sequence of a novel carbonic anhydrase-related polypeptide and its exclusive presence in Purkinje cells
3. Assignment of the gene for human carbonic anhydrase VIII (CA8) to chromosome 8q11→q12
4. Molecular characterization of the human carbonic anhydrase-related protein (HCA-RP VIII)
5. Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme
6. Structure and mechanism of carbonic anhydrase
7. The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C
8. Rate of exchange of water from the active site of human carbonic anhydrase C
9. Carbonic anhydrase: Oxygen-18 exchange catalyzed by an enzyme with rate-contributing proton-transfer steps
10. Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrase
11. Structure and denaturation of human carbonic anhydrases in urea and guanidine hydrochloride solutions
12. Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes
13. Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200
14. Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis
15. Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II
16. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
17. Hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle
18. Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
19. The catalytic mechanism of carbonic anhydrase: Hydrogen isotope effects on the kinetic parameters of the human C isoenzyme
20. Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
21. 2 hydration catalyzed by human carbonic anhydrase I
22. Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis
23. Carbonic anhydrase
24. 2 hydration catalyzed by human carbonic anhydrase II. Mechanistic implications
25. The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue
26. Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II
27. Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
28. Carbonic anhydrase and the role of orientation in catalysis
29. Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I
30. A comparison of the kinetic properties of native bovine muscle carbonic anhydrase and an activated derivative with modified thiol groups