Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus

Extremophiles

Volumn 6, Issue 4, 2002, Pages 283-289

  Iyer, Ramesh B ^a   Wang, Jianquan ^a   Bachas, Leonidas G ^a  

^a UNIVERSITY OF KENTUCKY   (United States)

Author keywords

Aquifex aeolicus; Cloning; Enzyme; Glucose 6 phosphate dehydrogenase; Thermophilic; Thermostability

Indexed keywords

AQUIFEX AEOLICUS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

GLUCOSE 6 PHOSPHATE DEHYDROGENASE; PRIMER DNA; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIUM; CATALYSIS; CHEMISTRY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIA; BASE SEQUENCE; CATALYSIS; CLONING, MOLECULAR; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENES, BACTERIAL; GLUCOSEPHOSPHATE DEHYDROGENASE; KINETICS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0036691498     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-001-0255-2     Document Type: Article

References (32)

1. Adams MWW (1993) Enzymes and proteins from organisms that grow near and above 100°C. Annu Rev Microbiol 47:627-658
2. Au SW, Gover S, Lam VM, Adams MJ (2000) Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Struct Fold Des 8:293-303
3. Burggraf S, Olsen GJ, Stetter KO, Woese CR (1992) A phylogenetic analysis of Aquifex pyrophilus. Syst Appl Microbiol 15:353-356
4. Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR (1998) On the mechanism of the reaction catalyzed by glucose-6-phosphate dehydrogenase. Biochemistry 37:2759-2767
5. Cosgrove MS, Gover S, Naylor CE, Vandeputten-Rutten L, Adams MJ, Levy HR (2000) An examination of the role of Asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase: x-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme. Biochemistry 39:15002-15011
6. Deckert G, Warren PV, Gaasterland T, Young WG, Lenox AL, Graham DE, Overbeek R, Snead MA, Keller M, Aujay M, Huber R, Feldman RA, Short JM, Olsen GJ, Swanson RV (1998) The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature (Lond) 392:353-358
7. Diruggiero J, Robb FT (1995) Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Appl Environ Microbiol 61:159-164
8. Feng D-F, Doolittle RF (1987) Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J Mol Evol 25:351-360
9. Fujita Y, Yoshida K, Miwa Y, Yanai N, Nagakawa E, Kasahara Y (1998) Identification and expression of the Bacillus subtilis fructose-1,6- bisphosphatase gene (fbp). J Bacteriol 180:4309-4313
10. Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PDB Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
11. Hirschbein BL, Whitesides GM (1982) Laboratory-scale enzymatic/chemical syntheses of D- and L-β-clorolactic acid and D- and L-potassium glycidate. J Am Chem Soc 104:4458-4460
12. Hosoda H, Fukuda K, Takahashi N, Goto J (1992) Use of the thermostable glucose-6-phosphate dehydrogenase as a label enzyme in steroid enzyme immunoassays. Chem Pharm Bull 40:294-295
13. Kasahara Y (1992) Homogeneous enzyme immunoassays. In: Nakamura RM, Kasahara Y, Rachnitz GA (eds) Immunochemical assays and biosensor technology for the 1990s. American Society for Microbiology, Washington, DC, pp 169-182
14. Kelly RM, Brown SH (1993) Enzymes from high-temperature microorganisms. Curr Opin Biotechnol 4:188-192
15. Kengen SW, Luesink EJ, Stams AJ, Zehnder AJ (1993) Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur J Biochem 213:305-312
16. Laderman KA, Asada K, Uemori T, Mukai H, Taguchi Y, Kato I, Anfinsen CB (1993) Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli. J Biol Chem 268:24402-24407
17. Lee WT, Levy HR (1992) Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. Protein Sci 1:329-334
18. Okuno H, Nagat K, Nakajima H (1985) Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus. J Appl Biochem 7:192-201
19. Olive C, Levy HR (1967) The preparation and some properties of crystalline glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Biochemistry 6:730-736
20. Peitsch MC (1995) Protein modeling by email. Biotechnology 13:658-660
21. Peitsch MC (1996) ProMod and Swiss-Model: Internet-based tools for automated comparative protein modeling. Biochem Soc Trans 24:274-279
22. Pitulle C, Yang Y, Marchiani M, Moore ER, Siefert JL, Aragno M, Jurtshuk P Jr, Fox GE (1994) Phylogenetic position of the genus Hydrogenobacter. Int J Syst Bacteriol 44:620-626
23. Rowland P, Basak, AK, Gover S, Levy HR, Adams MJ (1994) The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 Å resolution. Structure 2:1073-1087
24. Slein MW (1963) D-glucose, determination with hexokinase and glucose-6-phosphate dehydrogenase. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Academic Press, New York, p 117
25. Stetter KO (1996) Hyperthermophilic procaryotes. FEMS Microbiol Rev 18:149-158
26. Stetter KO (1998) Hyperthermophiles: isolation, classification and properties. In: Horikoshi K, Grant WD (eds) Extremophiles: microbial life in extreme environments. Wiley-Liss, New York, pp 1-24
27. Stetter KO, König H, Stackebrandt E (1983) Pyrodictium gen. nov., a new genus of submarine disk-shaped sulfur reducing archaebacteria growing optimally at 105°C. Syst Appl Microbiol 4:535-551
28. Tanahashi T, Tochikubo K, Hachisuka Y (1976) Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores. Jpn J Microbiol 20:281-286
29. Ujita S, Kimura K (1975) Studies of glucose metabolism in Bacillus subtilis. I. Purification of glucose-6-phosphate dehydrogenase from the vegetative cell and its properties in comparison with the spore enzyme. J Biochem 77:197-206
30. Wass JA (1999) GPMAW 4.0. Biotechnol Softw I J 16:14-17
31. Wong C-H, Whitesides GM (1981) Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and the glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. J Am Chem Soc 103:4890-4899
32. Yao T, Ogawa H, Nakahara T (1995) Highly selective and sensitive detection of NADP coenzymes using co-immobilized glucose-6-phosphate dehydrogenase/diaphorase reactors as on-line amplifiers based on substrate recycling in a chemiluminescence flow injection system. Talanta 42:1297-1303