Purification and properties of an extremely thermostable NADP+-specific glutamate dehydrogenase from Archaeoglobus fulgidus

Archives of Microbiology

Volumn 168, Issue 6, 1997, Pages 536-539

  Aalén, Nina ^a   Steen, Ida Helene ^a   Birkeland, Nils Kåre ^a   Lien, Torleiv ^a  

^a UNIVERSITY OF BERGEN   (Norway)

Author keywords

Amino acid dehydrogenase; Archaea; Archaeoglobus fulgidus; Glutamate dehydrogenase; Thermostable enzyme

Indexed keywords

GLUTAMATE DEHYDROGENASE;

ARCHAEBACTERIUM; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; THERMOSTABILITY;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; ARCHAEOGLOBUS FULGIDUS; ENZYME STABILITY; GLUTAMATE DEHYDROGENASE; HALF-LIFE; KINETICS; MOLECULAR SEQUENCE DATA; NADP; TEMPERATURE;

ARCHAEA; ARCHAEOGLOBUS FULGIDUS; PYROCOCCUS; THERMOCOCCUS;

EID: 0030730997     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050533     Document Type: Article

References (21)

1. Beeder J, Nilsen RK, Rosnes JT, Torsvik T, Lien T (1994) Archaeoglobus fulgidus isolated from hot North Sea oil field waters. Appl Environ Microbiol 60:1227-1231
2. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
3. Britton KL, Baker PJ, Borges KMM, Engel PC, Pasquo A, Rice DW, Robb FT, Scandurra R, Stillman TJ, Yip KSP (1995). Insights into the thermal stability from a comparison of the glutamate dehydrogenase from Pyrococcus furiosus and Thermococcus litoralis. Eur J Biochem 229:688-695
4. Consalvi V, Chiaraluce R, Politi L, Gambacorta A, De Rosa M, Scandurra R (1991a) Glutamate dehydrogenase from the thermophilic archaebacterium Sulfolobus solfataricus Eur J Biochem 196:459-467
5. Consalvi V, Chiaraluce R, Politi L, Vaccaro R, De Rosa M, Scandurra R (1991b) Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Eur J Biochem 202:1189-1196
6. Consalvi V, Chiaraluce R, Millevoi S, Pasquo A, Politi L, De Rosa M, Scandurra R (1994) NAD-dependent glutamate dehydrogenase from the thermophilic eubacterium Bacillus acidocaldarius. Comp Biochem Physiol 109B:691-699
7. Fabry S, Hensel R (1987) Purification and characterization of the D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus. Eur J Biochem 165:147-155
8. Ferrer J, Pérez-Pomares F, Bonete MJ (1996) NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability. FEMS Microbiol Lett 141:59-6
9. Hudson RC, Daniel RM (1993) L-glutamate dehydrogenases: distribution, properties and mechanism. Comp Biochem Physiol 106B:767-792
10. 10-methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri. Arch Microbiol 159:213-219
11. Kobayashi T, Higuchi S, Kimura K, Kudo T, Horikoshi K (1995) Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus. J Biochem 118:587-592
12. Kunow J, Linder D, Thauer RK (1995) Pyruvate:ferredoxin oxidoreductase from the sulfate-reducing Archaeoglobus fulgidus: molecular composition, catalytic properties, and sequence alignments. Arch Microbiol 163:21-28
13. Langelandsvik AS, Steen IH, Birkeland NK, Lien T (1997) Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus. Arch Microbiol 168:59-67
14. Ma K, Robb FT, Adams MWW (1994) Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis. Appl Environ Microbiol 60:562-568
15. 420 in Archaeoglobus fulgidus. Arch Microbiol 152:362-368
16. Ohshima T, Nishida N (1993) Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus. Biosci Biotechnol Biochem 57:945-951
17. Ohshima T, Nishida N (1994) Purification and characterization of extremely thermostable glutamate dehydrogenase from a hyperthermophilic archaeon, Thermococcus litoralis. Biocatalysis 11:117-129
18. Robb FT, Park JB, Adams MWW (1992) Characterization of an extremely thermostable glutamate dehydrogenase; a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium Pyrococcus furiosus. Biochim Biophys Acta 1120:267-272
19. 10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea. Arch Microbiol 159:225-232
20. 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus. Arch Microbiol 163:112-118
21. Yip KSP, Stillman TJ, Britton KL, Artyiuk PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Scandurra R, Rice DW (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