Crystallization and characterization of bovine liver glutamate dehydrogenase

Journal of Structural Biology

Volumn 120, Issue 1, 1997, Pages 73-77

  Peterson, Peter E ^a   Pierce, Jonathan ^a   Smith, Thomas J ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; GLUTAMATE DEHYDROGENASE;

ANIMAL CELL; ARTICLE; CATTLE; CRYSTALLIZATION; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME ANALYSIS; MAMMAL; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL;

EID: 0031257724     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3899     Document Type: Article

References (34)

1. Alex S., Bell J. E. Dual nucleotide specificity of bovine glutamate dehydrogenase: The role of negative cooperativity. Biochem. J. 191:1980;299-304.
2. Appella E., Tomkins G. M. The subunits of bovine liver glutamate dehydrogenase: Demonstration of a single peptide chain. J. Mol. Biol. 18:1966;77-89.
3. Bailey J. S., Bell E. T., Bell J. E. Regulation of bovine glutamate dehydrogenase. J. Biol. Chem. 257:1982;5579-5583.
4. Baker P. J., Britton K. L., Engel P. C., Farrants G. W., Lilley K. S., Rice D. W., Stillman T. J. Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins. 12:1992a;75-86.
5. Baker P. J., Britton K. L., Rice D. W., Rob A., Stillmann T. J. Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. J. Mol. Biol. 228:1992b;662-671.
6. Bayley P. M., O'Neill T. J. The binding of oxidised coenzyme to bovine-liver glutamate dehydrogenase studied by circular-difference spectroscopy. Eur. J. Biochem. 112:1980;521-531.
7. ++. Biochim. Biophys. Acta. 309:1973;237-242.
8. Colman R. F., Frieden C. Cooperative Interaction between the GTP sites of glutamate dehydrogenase. Biochem. Biophys. Res. Commun. 22:1966;100-105.
9. Dalziel K., Egan R. R. The binding of oxidized coenzymes by glutamate dehydrogenase and the effects of glutarate and purine nucleotides. Biochem. J. 126:1972;975-984.
10. Egan R. R., Dalziel K. Active centre equivalent weight of glutamate dehydrogenase from dry weight determinations and spectrophotometric titrations of abortive complexes. Biochim. Biophys. Acta. 250:1971;47-50.
11. Engel P., Dalziel K. Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Biochem. J. 115:1969;621-631.
12. Engel P. C., Chen S. A product-inhibition study of bovine liver glutamate dehydrogenase. Biochem. J. 151:1975;305-318.
13. Fisher H. F., Cross D., McGregor L. L. Catalytic activity of subunits of glutamic dehydrogenase. Nature. 196:1962;895-896.
14. Frieden C. The dissociation of glutamate dehydrogenase by reduced diphosphopyridine nucleotide (DPNH). Biochim et Biophys. Acta. 27:1958;431-432.
15. Frieden C. Glutamic dehydrogenase I. The effect of coenzyme on the sedimentation velocity and kinetic mechanism. J. Biol. Chem. 234:1959a;809-814.
16. Frieden C. Glutamic dehydrogenase II The effect of various nucleotides on the association-disassociation and kinetic properties. J. Biol. Chem. 234:1959b;815-819.
17. Frieden C. Different structural forms of reversibly dissociated glutamic dehydrogenase: Relation between enzymatic activity and molecular weight. Biochem. Biophys. Res. Commun. 10:1963a;410-415.
18. Frieden C. L. 1963b;Academic Press, New York.
19. George S. A., Bell J. E. Effects of adenosine 5′-diphosphate on bovine glutamate dehydrogenase: Diethyl pyrocarbonate modification. Biochemistry. 19:1980;6057-6061.
20. Iwatsubo M. a. P. D. Regulation De L'Activite' De La glutamate dehydrogenase par les effecteurs GTP et ADP: ETUDE par "stopped flow," Bull. Soc. Chem. Biol. 49:1967;1563-1572.
21. Josephs R., Eisenberg H. Biopolymers. 9:1970;877-889.
22. Josephs R., Eisenberg H., Reisler E. Some properties of crosslinked polymers of glutamic dehydrogenase. Biochemistry. 12:1973;4060-4067.
23. Koberstein R., Sund H. The influence of ADP, GTP and L-glutamate on the binding of the reduced coenzyme to beef-liver glutamate dehydrogenase. Eur. J. Biochem. 36:1973;545-552.
24. Limuti C. M. Glutamate Dehydrogenase: Equilibrium and Kinetic Studies. 1983;Univ. of Rochester, Rochester.
25. Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
26. Olsen J. A., Anfinsen C. B. The crystallization and characterization of L-glutamic acid dehydrogenase. J. Biol. Chem. 197:1952;67-79.
27. Otwinoski Z. Sawyer L., Isaacs N., Bailey S. DENZO. 1993;56-62 SERC Daresbury Laboratory, Warrington.
28. Rice D. W., Baker P. J., Farrants G. W., Hornby D. P. The crystal structure of glutamate dehydrogenase from Clostridium symbiosum at 0.6 nm resolution. Biochem. J. 242:1987;789-795.
29. C. A. Smith, G. E. Norris, E. N. Baker, 1996, The structure of the thermophilic glutamate dehydrogenase fromThermococcus, A52, C 226, 227.
30. Smith E. J., Landon M., Piszkiewicz D., Brattin W. J., Langley T. J., Melamed M. D. Bovine liver glutamate dehydrogenase: Tentative amino acid sequence; identification of a reactive lysine; nitration of a specific tyrosine and loss of allosteric inhibition by guanosine triphosphate. Proc. Natl. Acad. Sci. USA. 67:1970;724-730.
31. Smith T. J., Bell J. E. The mechanism of hysteresis in bovine glutamate dehydrogenase: The role of subunit interactions. Biochem. 21:1982;733-737.
32. Stillman T. J., Baker P. J., Britton K. L., Rice D. W. Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J. Mol. Biol. 234:1993;1131-1139.
33. Tong L., Rossmann M. G. The locked rotation function. Acta Crystallogr. A46:1990;783-792.
34. 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. W. The structure ofPyrococcus furiosus. Structure. 3:1995;1147-1158.