Biochemistry: How active sites communicate in thiamine enzymes

Science

Volumn 306, Issue 5697, 2004, Pages 818-820

  Jordan, Frank ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

THIAMINE;

BIOCHEMISTRY;

CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN BOND; INTERPERSONAL COMMUNICATION; KINETICS; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SHORT SURVEY;

AMINO ACID SUBSTITUTION; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE; DIMERIZATION; GLUTAMIC ACID; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTONS; PYRUVATE DEHYDROGENASE (LIPOAMIDE); PYRUVATE DEHYDROGENASE COMPLEX; THIAMINE PYROPHOSPHATE;

ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; MAMMALIA;

EID: 7444254990     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1105457     Document Type: Short Survey

References (11)

1. K. E. Neet, in Contemporary Enzyme Kinetics and Mechanism, D. L. Purich, Ed. (Academic Press, New York, 1983), pp. 267-320.
2. R. A. W. Frank, C. M. Titman, J. V. Pratap, B. F. Luisi, R. N. Perham, Science 306, 872 (2004).
3. The E1 subunit is an example of the second class, with an α2β2 tetramer; the E2 subunit appears to resist multiple efforts at crystallization, and hence for this structure a "divide and conquer" approach was used, including NMR and x-ray studies.
4. L. S. Khailova, L. G. Korochkina, Biochem. Int. 11, 509 (1985).
5. E. M. Ciszak et al., J. Biol. Chem. 278, 21240 (2003).
6. For a review of the enzymes discussed in this Perspective, see F. Jordan, M. Patel, Eds., Thiamine: Catalytic Mechanisms and Role in Normal and Disease States (Marcel Dekker, New York, 2004), pp. 1-588.
7. D. Kern et al., Science 275, 67 (1997).
8. N. Nemeria et al., Biochemistry 43, 6565 (2004).
9. P. Arjunan et al., Biochemistry 41, 5213 (2002).
10. P. Arjunan et al., J. Mol. Biol. 256, 590 (1996).
11. Work in the author's laboratory is supported by U.S. Public Health Service (grants NIH GM-50380 and NIH GM-62330).