Sequence similarities of glyceraldehyde-3-phosphate dehydrogenases, phosphoglycerate kinases, and pyruvate kinases are species optimal temperature-dependent

European Biophysics Journal

Volumn 27, Issue 4, 1998, Pages 409-410

  Early, Cathleen N ^a   Britt, B Mark ^a  

^a BAYLOR UNIVERSITY   (United States)

Author keywords

Evolution; Glyceraldehyde 3 phosphate dehydrogenase; Phosphoglycerate kinase; Phylogeny; Pyruvate kinase; Sequence similarity

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PHOSPHOGLYCERATE KINASE; PYRUVATE KINASE;

ARTICLE; BACTERIUM; BIRD; EVOLUTION; MAMMAL; PHYLOGENY; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; TEMPERATURE DEPENDENCE;

ANIMALS; BIOPHYSICS; EVOLUTION, MOLECULAR; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HUMANS; PHOSPHOGLYCERATE KINASE; PYRUVATE KINASE; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; TEMPERATURE;

AVES; BACTERIA (MICROORGANISMS); MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0031850774     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050148     Document Type: Article

References (11)

1. Bairoch A, Apweiler R (1996) The SWISS-PROT protein sequence data bank and its new supplement TREMBL. Nucleic Acids Res 24:21-25
2. Bevington PR (1969) Data reduction and error analysis for the physical sciences. McGraw-Hill, New York
3. Britt BM (1993) A shifting specificity model for enzyme catalysis. J Theor Biol 164:181-190
4. Britt BM (1997) For enzymes, bigger is better. Biophys Chem 69:63-70
5. Castro C, Britt BM (1998) Evidence for a low temperature transition state binding preference in bovine adenosine deaminase. Biophys Chem 70:87-92
6. Hensel R, Zwickl P, Fabry S, Lang J, Palm P (1989) Sequence comparison of glyceraldehyde-3-phosphate dehydrogenases from the three urkingdoms: evolutionary implication. Can J Microbiol 35:81-85
7. Holt JG, Krieg NR, Sneath PHA, Staley JT, Williams ST (1994) Bergey's manual of determinative bacteriology, 9th edn. Williams and Wilkins, Baltimore
8. Martin W, Cerff R (1986) Prokaryotic features of a nucleus-encoded enzyme: cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from mustard (Sinapis alba) Eur J Biochem 159:323-331
9. Menendez-Arias L, Argos P (1989) Engineering protein thermal stability: sequence statistics point to residue substitutions in α-helices. J Mol Biol 206:397-406
10. Rodbard S (1950) Weight, body temperature. Science 111:465-466
11. Wang T S-F, Wong SW, Korn D (1989) Human DNA polymerase α: predicted functional domains and relationships with viral DNA polymerases. FASEB J 3:14-21