Stability, catalytic versatility and evolution of the (βα)8-barrel fold

Current Opinion in Biotechnology

Volumn 12, Issue 4, 2001, Pages 376-381

  Höcker, Birte ^a   Jürgens, Catharina ^a   Wilmanns, Matthias ^b   Sterner, Reinhard ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PROTEIN;

CATALYSIS; ENZYME SPECIFICITY; MOLECULAR EVOLUTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; THERMOSTABILITY;

EID: 0035423614     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(00)00230-5     Document Type: Review

References (39)

1. Enabling the chemistry of life
2. Extremozymes
3. Thermophilic adaptation of proteins
4. Barrels in pieces?
5. The TIM-barrel fold: A versatile framework for efficient enzymes
6. TIM barrel fold: Structural, functional and evolutionary characteristics in natural and designed molecules
7. Design by necessity
8. Trp operon
9. Phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima is an extremely stable and active homodimer
10. Crystal structure at 2.0 Å resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: Possible determinants of protein stability
11. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
12. 2.0 Å Structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
13. The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges
14. Structural and mutagenesis studies of Leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
15. How enzymes adapt: Lessons from directed evolution
16. 8-barrel fold
17. Breaking open a protein barrel
18. Characteristics of a de novo designed protein
19. 8 polypeptides designed for investigating the influence of β-residue packing on the α/β-barrel structure stability
20. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
21. Improving the catalytic activity of a thermophilic enzyme at low temperatures
22. The enolase superfamily: A general strategy for enzyme-catalysed abstraction of the α-protons of carboxylic acids
23. Unexpected divergence of enzyme function and sequence: 'N-acylamino acid racemase' is o-succinylbenzoate synthase
24. 2+ and o-succinylbenzoate
25. New functions from old scaffolds: How nature reengineers enzymes for new functions
26. Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (Loop 8) of triosephosphate isomerase: Toward a new substrate specificity
27. Alkaliphiles - From an industrial point of view
28. X-ray structure of Novamyl, the five-domain 'maltogenic' α-amylase from Bacillus stearothermophilus: Maltose and acarbose complexes at 1.7 Å resolution
29. Conversion of the maltogenic α-amylase Novamyl into a CGTase
30. Directed evolution of new catalytic activity using the α/β-barrel scaffold
31. Structural evidence for evolution of the β/α barrel scaffold by gene duplication and fusion
32. 8-barrel enzyme to catalyse related reactions in two different metabolic pathways
33. A histidine gene cluster of the hyperthermophilic Thermotoga maritima: Sequence analysis and evolutionary significance
34. 8-barrel enzyme into two folded halves
35. On the ancestry of barrels
36. 8-barrels: Implications for the evolution of metabolic pathways
37. Structural proteomics: Prospects for high throughput sample preparation