Temperature dependence of the enzyme-substrate recognition mechanism

Journal of Biochemistry

Volumn 129, Issue 1, 2001, Pages 173-178

  Ura, Hideaki ^a   Harata, Kazuaki ^b   Matsui, Ikuo ^b   Kuramitsu, Seiki ^a,b,c,d  

^a OSAKA UNIVERSITY   (Japan)

^b NATL INST BIOSCI HUM TECHNOL   (Japan)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

^d RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

Aminotransferase; Domain movement; Hyperthermophilic enzyme; Pyrococcus horikoshii; Substrate recognition

Indexed keywords

AMINOTRANSFERASE;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; HYDROGEN BOND; LIGAND BINDING; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN DOMAIN; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMOSTABILITY; THERMUS THERMOPHILUS;

ANIMALIA; ESCHERICHIA COLI; PYROCOCCUS HORIKOSHII; THERMUS THERMOPHILUS;

EID: 0035129237     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a002829     Document Type: Article

References (35)

1. Evolutionary relationships among aminotransferases Tyrosine aminotransferase, histidinol-phosphate aminotranferase, and aspartate aminotransferase are homologous proteins
2. The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent
3. Energestics of protein structure
4. Protein thermal stability, hydrogen bonds, and ion pairs
5. Factors enhancing protein thermostability
6. The stability of proteins in extreme environments
7. Directed evolution of thermostable kanamycin-resistance gene: A convenient selection marker for Thermus thermophilus
8. A general rule for the relationship between hydrophobic effect and conformational stability of a protein: Stability and structure of a series of hydrophobic mutants of human lysozyme
9. Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme
10. X-ray crystallographic study of pyridoxamine 5′-phosphate-type aspartate aminotransferases from Escherichia coli in three forms
11. X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form
12. Free energy requirement for domain movement of an enzyme
13. An aspartate aminotransferase from an extremely thermophilic bacterium. Thermus thermophilus HBS
14. Structure of Thermus thermophilus HB8 aspartate aminotransfersase and its complex with maleate
15. The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii
16. The synthesis and properties of phosphopylidoxyl amino acids
17. The CCP4 suite: Programs from protein crystallography
18. AMoRe: An automated package for molecular replacement
19. Crystallographic R factor refinement by molecular dynamics
20. Simulated annealing in crystallography
21. Accurate bond and angle parameters for X-ray protein structure refinement
22. Improved methods for building protein models in electron density maps and the location of errors in these models
23. PROCHECK-A program to check the stereochemical quality of protein structures
24. Raster 3D version 2.0: A program for photorealistic molecular graphics
25. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
26. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
27. The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8
28. The electrostatic effects in the ionization of weak acids in water and wate@dioxane mixtures
29. The 2.1 Å crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II) B core/TATA-box
30. Co-crystal structure of TBP recognizing the minor groove of a TATA element
31. Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: Archaeon specificity and catalytic mechanism of adenylate formation
32. The free yeast aspartyl-tRNA synthetase differs from the tRNA (Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain