Enzyme catalysis: Removing chemically 'essential' residues by site-directed mutagenesis

Trends in Biochemical Sciences

Volumn 26, Issue 8, 2001, Pages 497-503

  Peracchi, Alessio ^a  

^a UNIVERSITY OF PARMA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; FRUCTOSE 2,6 BISPHOSPHATASE; GLUCAN 1,4 ALPHA GLUCOSIDASE; RIBONUCLEASE T1; STEROID DELTA ISOMERASE; SUBTILISIN;

CATALYSIS; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; NONHUMAN; PLASTICITY; POINT MUTATION; PRIORITY JOURNAL; REVIEW; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; ENZYMES; MUTAGENESIS, SITE-DIRECTED;

EID: 0035425380     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01911-9     Document Type: Review

References (49)

1. A proficient enzyme
2. Site directed mutagenesis
3. Tinkering with enzymes: What are we learning?
4. Site-directed mutagenesis: A tool for studying enzyme catalysis
5. Identification of the histidine and aspartic acid residues essential for enzymatic activity of a family I.3 lipase by site-directed mutagenesis
6. 1. Atomic dissection of the enzyme substrate interactions
7. 1 acts as a base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine
8. 1 as studied by double and triple mutants
9. 1 with asparagine and glutamine replacements: Analysis of double mutant cycles at one position
10. 1: Concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond
11. 5-steroid isomerase
12. 5-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization
13. 5-3-ketosteroid isomerase
14. 5-steroid isomerase: Recruitment of aspartate-99 as the base
15. Glucoamylase: Structure/function relationships, and protein engineering
16. Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori
17. Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the γ-carboxylate group of glutamic acid 400
18. Dissecting the catalytic triad of a serine protease
19. Functional interaction among catalytic residues in subtilisin BPN′
20. Catalytic properties of class A β-lactamases: Efficiency and diversity
21. Enzyme-induced strain/distortion in the ground-state ES complex in β-lactamase catalysis revealed by FTIR
22. Active-site serine mutants of the Streptomyces albus G β-lactamase
23. Reaction mechanism of fructose-2,6-bisphosphatase. A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway
24. Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities
25. Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase
26. Binding energy, specificity and enzymic catalysis: The Circe effect
27. Substrate-assisted catalysis: Molecular basis and biological significance
28. Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
29. Nucleophilic activation by positioning in phosphoryl transfer catalyzed by nucleoside diphosphate kinase
30. Chemical rescue of phosphoryl transfer in a cavity mutant: A cautionary tale for site-directed mutagenesis
31. From β-glucanase to β-glucansynthase: Glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile
32. Reviving a dead enzyme: Cytosine deaminations promoted by an inactive DNA methyltransferase and an S-adenosylmethionine analogue
33. Catalytic promiscuity and the evolution of new enzymatic activities
34. Evolutionary conservation of enzymatic catalysis: Quantitative comparison of the effects of mutation of aligned residues in Saccharomyces cerevisiae and Escherichia coli inorganic pyrophosphatases on enzymatic activity
35. Structure and kinetics of the β-lactamase mutants S70A and K73H from Staphylococcus aureus PC1
36. Unnatural amino acids as probes of protein structure and function
37. Analysis of the role of the active site tyrosine in human glutathione transferase A1-1 by unnatural amino acid mutagenesis
38. Identification of enzyme-substrate and enzyme-product complexes in the catalytic mechanism of glucoamylase from Aspergillus awamori
39. Tailoring new enzyme functions by rational redesign
40. Mechanism of adenylate kinase. What can be learned from a mutant enzyme with minor perturbation in kinetic parameters?
41. Ambiguities in mapping the active site of a conformationally dynamic enzyme by directed mutation. Role of dynamics in structure-function correlations in Escherichia coli adenylosuccinate synthetase
42. A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease
43. Kinetics of RNA degradation by specific base catalysis of transesterification involving the 2′-hydroxyl group
44. Acid-catalyzed hydrolysis of maltosyl-β-cyclodextrin
45. Determination of the microscopic rate constants for the base-catalyzed conjugation of 5-androstene-3,17-dione
46. Chemical reactivity of penicillins and cephalosporins. Intramolecular involvement of the acyl-amido side chain
47. The reactivity of phosphate esters. Monoester hydrolysis