The esterase from the thermophilic eubacterium Bacillus acidocaldaris: Structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus

Proteins: Structure, Function and Genetics

Volumn 40, Issue 3, 2000, Pages 473-481

  D'Auria, Sabato ^a,c   Herman, Petr ^a   Lakowicz, Joseph R ^a   Tanfani, Fabio ^b   Bertoli, Enrico ^b   Manco, Giuseppe ^c   Rossi, Mose' ^c  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

^c INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Anisotropy decays; Frequency domain fluorometry; Infrared; Protein stability; Protein structure; Thermophilic enzyme

Indexed keywords

ACRYLAMIDE; CARBOXYLESTERASE; ESTERASE;

ARCHAEBACTERIUM; ARCHAEOGLOBUS FULGIDUS; ARTICLE; BACILLUS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; TEMPERATURE SENSITIVITY; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

ARCHAEOGLOBUS FULGIDUS; BACILLUS; CARBOXYLIC ESTER HYDROLASES; COMPARATIVE STUDY; ENZYME STABILITY; FLUORESCENCE POLARIZATION; HEAT; PLIABILITY; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TRYPTOPHAN;

ALICYCLOBACILLUS ACIDOCALDARIUS; ARCHAEA; ARCHAEOGLOBUS; ARCHAEOGLOBUS FULGIDUS; BACILLUS ACIDOCALDARIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 0034663653     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20000815)40:3<473::AID-PROT140>3.0.CO;2-8     Document Type: Article

References (44)

1. The lessons of archaebacteria
2. Hyperthermophilic microorganisms
3. Enzymes and proteins from orgnisms that grow near and above 100 °C
4. Structure-function studies on β-glycosidase from Sulfolobus solfataricus. Molecular bases of thermostability
5. Engineering an enzyme to resist boiling
6. Enzymes from thermophilic archaebacteria: Current and future apphcations in biotechnology
7. How do enzymes work?
8. Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2
9. How to make my blood boil
10. Solution structure and DNA binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
11. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pairs networks in maintaining enzyme stability at extreme temperatures
12. Native protein fluctuations: The conformational motions temperature and the inverse correlation of protein flexibility with protein stability
13. Biochemistry
14. The denaturation and degradation of stable enzymes at high temperature
15. Stability and dynamics in a hyperthermophilic protein with melting point close to 200°C
16. Fluorescence studies with tryptophan analogues: Excited state interactions involving the side-chain amino groups
17. Micro-environmental effects on the solvent quenching rate in constrained tryptophan derivatives
18. The thermophilic esterase from Archaeoglobus fulgidus: Structure and conformational dynamics at high temperature
19. Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily
20. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
21. Frequency-domain fluorescence spectroscopy
22. Review of fluorescence anisotropy decay analysis by frequency-domain fluorescence spectroscopy
23. Infrared measurements of peptide hydrogen exchange in rhodopsin
24. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
25. Quantitative studies of the structure of proteins in solutions by Fourier-transform infrared spectroscopy
26. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
27. Determination of protein secondary structure using factor analysis of infrared spectra
28. Effects of temperature and SDS on the structure of β-glycosidase from the thermophilic archaeon Sulfolobus solfataricus
29. Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli
30. Structural-functional relationships in pig hearth AMP-deaminase in the presence of ATP, orthophosphate, and phosphatidate bilayers
31. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
32. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
33. Fluorescence quenching of indole and model micelle systems
34. Does the fluorescence quencher acrylamide bind to proteins?
35. The β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Enzyme activity and conformational dynamics at temperatures above 100°C
36. A 10 GHz frequency-domain fluorometer
37. Analysis of fluorescence decay kinetic from variable frequency phase shifts and modulation data
38. Time-resolved fluorescence anisotropies of fluorophores in solvents and lipid bilayers obtained from frequency-domain phase modulation fluorometry
39. Anisotropy decays of indole, mellitin monomer and mellitin tetramer by frequency-domain fluorometry and multi-wavelength global analysis
40. Anisotropy decays of single tryptophan proteins measured by GHz frequency-domain fluorometry with collisional quenching
41. 1L(b) transitions and comparison with theory
42. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
43. Photophysics of aqueus tryptophan: pH and temperature effects