NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1: Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases

European Journal of Biochemistry

Volumn 267, Issue 1, 2000, Pages 121-131

  Di Fraia, Raffaela ^a   Wilquet, Valerie ^b   Ciardiello, M Antonietta ^a   Carratore, Vito ^a   Antignani, Antonella ^a   Camardella, Laura ^a   Glansdorff, Nicolas ^b,c   Di Prisco, Guido ^a,d  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b Jean Marie Wiame Inst M   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^d CNR   (Italy)

Author keywords

Antarctic; Gene sequence; Glutamate dehydrogenase; Protein sequence; Psychrotolerant bacterium

Indexed keywords

BACTERIAL ENZYME; GLUTAMATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIOLOGY; CATALYSIS; DNA SEQUENCE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANTARCTIC REGIONS; BASE SEQUENCE; CLONING, MOLECULAR; CODON; ENZYME STABILITY; GAMMAPROTEOBACTERIA; GLUTAMATE DEHYDROGENASE (NADP+); GRAM-NEGATIVE AEROBIC RODS AND COCCI; HYDROGEN-ION CONCENTRATION; KETOGLUTARIC ACIDS; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NADP; OPEN READING FRAMES; PROMOTER REGIONS (GENETICS); SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

EID: 0033962829     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.00972.x     Document Type: Article

References (41)

1. 1. Somero, G.N. & Hochachka, P.W. (1968) The effect of temperature on catalytic and regulatory functions of pyruvate kinases of the rainbow trout and the Antarctic fish Trematomus bernacchii. Biochem. J. 110, 395-400.
2. 2. Hochachka, P.W. & Somero, G.N. (1984) Biochemical Adaptation. Princeton University Press, Princeton, NJ.
3. 3. Kobori, H., Sullivan, C.W. & Shizuya, H. (1984) Heat-labile alkaline phosphatase from Antarctic bacteria: rapid 5′ end-labelling of nucleic acids. Proc. Natl Acad. Sci. USA 81, 6691-6695.
4. 4. Vckovski, V., Schlatter, D. & Zuber, H. (1990) Structure and function of L-lactate dehydrogenase from thermophilic, mesophilic and psychrophilic bacteria, IX. Identification, isolation and nucleotide sequence of two L-lactate dehydrogenase genes of the psychrophilic bacterium. Bacillus psychrosaccharolyticus. Biol. Chem. Hoppe-Seyler 371, 103-110.
5. 5. Rentier-Delrue, F., Mande, S.C., Moyens, S., Terpstra, P., Mainfroid, V., Goraj, K., Lion, M., Hol, W.G. & Martial, J. (1993) Cloning and overexpression of the triose phosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequence. J. Mol. Biol. 229, 85-93.
6. 6. Smalås, A.O., Heimstad, E.S., Hordvik, A., Willasen, N.P. & Male, R. (1994) Cold adaptation of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20, 149-166.
7. 7. Somero, G.N. (1995) Proteins and temperature. Annu. Rev. Physiol. 57, 43-68.
8. 8. Ciardiello, M.A., Camardella, L. & di Prisco, G. (1995) Glucose-6-phosphate dehydrogenase from the blood cells of two Antarctic teleosts: correlation with cold adaptation. Biochim. Biophys. Acta 1250, 76-82.
9. 9. Ciardiello, M.A., Camardella, L., Carratore, V. & di Prisco, G. (1997) Enzymes in Antarctic fish: glucose-6-phosphate dehydrogenase and glutamate dehydrogenase. Comp. Biochem. Physiol. 119A, 1031-1036.
10. 10. Genicot, S., Rentier-Delrue, F., Edwards, D., Van Beeumen, J. & Gerday, C. (1996) Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation. Biochim. Biophys. Acta 1298, 45-57.
11. 11. Feller, G., Narinx, E., Arpigny, J.L., Aittaleb, M., Baise, E., Genicot, S. & Gerday, C. (1996) Enzymes from psychrophilic organisms. FEMS Microbiol. Rev. 18, 189-202.
12. 12. Gerike, U., Danson, M.J., Russell, N.J. & Hough, D.W. (1997) Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur. J. Biochem. 248, 49-57.
13. 13. Alvarez, M., Zeelen, J.P., Mainfroid, V., Rentier-Delrue, F., Martial, J.A., Wyns, L., Wierenga, R.K. & Maes, D. (1998) Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. J. Biol. Chem. 273, 2199-2206.
14. 14. Tsigos, I., Velonia, K., Smonou, I. & Bouriotis, V. (1998) Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Eur. J. Biochem. 254, 356-362.
15. 15. Smith, E.L., Austen, B.M., Blumenthal, K.M. & Nyc, J.F. (1975) Glutamate dehydrogenases. In The Enzymes (Boyer, P.D., ed.), Vol. XI, pp. 293-367. Academic Press, New York.
16. 16. Hudson, R.C. & Daniel, R.M. (1993) L-Glutamate dehydrogenase: distribution, properties and mechanism. Comp. Biochem. Physiol. 106B, 767-792.
17. 17. DiRuggiero, J. & Robb, F.T. (1996) Enzymes of central nitrogen metabolism from hyperthermophiles: characterization, thermostability, and genetics. Adv. Protein Chem. 48, 311-339.
18. 18. Baker, P.J., Britton, K.L., Engel, P.C., Farrants, G.W., Lilley, K.S., Rice, D.W. & Stillman, T.J. (1992) Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins 12, 75-86.
19. 19. Knapp, S., de Vos, W.M., Rice, D. & Ladenstein, R. (1997) Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution. J. Mol. Biol. 267, 916-932.
20. 20. Yip, K.S.P., Stillman, T.J., Britton, K.L., Artymiuk, P.J., Baker, P.J., Sedelnikova, S.E., Engel, P.C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R. & Rice, D. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3, 1147-1158.
21. 21. Glansdorff, N. (1965) Topography of cotransducible arginine mutations in Escherichia coli K-12. Genetics 51, 167-179.
22. 22. Sambrook, J., Fritsch, E.F. & Maniatis, T. (1989) Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA.
23. 23. Veronese, F.M., Boccu, E. & Conventi, L. (1975) Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme. Biochim. Biophys. Acta 377, 217-228.
24. 24. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
25. 25. Camardella, L., Carratore, V., Ciardiello, M.A., Damonte, G., Benatti, U. & De Flora, A. (1995) Primary structure of human erythrocytes nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse turn transplantation antigen P35B. Blood 85, 264-267.
26. 26. Ramseier, T.M., Nègre, D., Cortay, J.-C., Scarabel, M., Cozzone, A.J. & Saier, M.H. Jr (1993) In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium. J. Mol. Biol. 234, 28-44.
27. 27. Sanger, F., Nicklen, S. & Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74, 5463-5467.
28. 28. Ikemura, T. (1981) Correlation between the abundance of Escherichia coli transfer RNAs and the occurence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system. J. Mol. Biol. 151, 389-409.
29. 29. Maras, B., Consalvi, V., Chiaraluce, R., Politi, L., De Rosa, M., Bossa, F., Scandurra, R. & Barra, D. (1992) The protein sequence of glutamate dehydrogenase from Sulfolobus solfataricus, a thermoacidophilic archaebacterium. Is the presence of N-ε-methyllysine related to thermostability? Eur. J. Biochem. 203, 81-87.
30. 30. Maras, B., Valiante, S., Chiaraluce, R., Consalvi, V., Politi, L., De Rosa, M., Bossa, F., Scandurra, R. & Barra, D. (1994) The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium. J. Protein Chem. 13, 253-259.
31. 31. Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
32. 32. Morita, R.Y. (1975) Psychrophilic bacteria. Bacteriol. Rev. 39, 144-167.
33. 33. Feller, G., Thiry, M., Arpigny, J.L. & Gerday, C. (1991) Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic Antarctic strain Moraxella TA144. Gene 102, 111-115.
34. 34. Feller, G., Payan, F., Theys, F., Qian, M., Haser, R. & Gerday, C. (1994) Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem. 222, 441-447.
35. 35. Sun, K., Camardella, L., di Prisco, G. & Hervé, G. (1998) Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica. FEMS Microbiol. Lett. 164, 375-382.
36. 36. Xu, Y., Zhang, Y., Liang, Z., Van de Casteele, M., Legrain, C. & Glansdorff, N. (1998) Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: properties of the enzyme, genetic organization and synthesis in Escherichia coli. Microbiology 144, 1435-1441.
37. 37. Benachenhou-Lahfa, N., Forterre, P. & Labedan, B. (1993) Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. J. Mol. Evol 36, 335-346.
38. 38. Kort, R., Liebl, W., Labedan, B., Forterre, P., Eggen, R.I.L. & de Vos, W. (1997) Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications. Extremophiles 1, 52-60.
39. 39. Wierenga, R.K., De Mayer, M.C.H. & Hol, W.G.J. (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding protein. Biochemistry 24, 1346-1357.
40. 40. Teller, J.K., Smith, R.J., McPherson, M.J., Engel, P.C. & Guest, J.R. (1992) The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli. Eur. J. Biochem. 206, 151-159.
41. 41. Stillman, T.J., Baker, P.J., Britton, K.L. & Rice, D.W. (1993) Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J. Mol. Biol. 234, 1131-1139.