Active form of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase

Biochemical and Molecular Medicine

Volumn 61, Issue 1, 1997, Pages 114-120

  Rogers, Kenneth S ^a   Rodwell, Victor W ^a   Geiger, Paul ^b  

^a PURDUE UNIVERSITY   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; BACTERIAL ENZYME; GLUTAMINE; HISTIDINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LYSINE; MUTANT PROTEIN;

ARTICLE; CALCULATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; NONHUMAN; PSEUDOMONAS;

BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS MEVALONII;

EID: 0031171975     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1997.2596     Document Type: Article

References (40)

1. 1. Beach MJ, Rodwell VW. Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Bacteriol 171:2994-3001, 1989.
2. 2. Lawrence CM, Chi Y-I, Rodwell VW, Stauffacher CV. Crystallization of HMG-CoA reductase from Pseudomonas mevalonii. Acta Crystallogr Sect D 51:386-389, 1995.
3. 3. Lawrence CM, Rodwell VW, Stauffacher CV. Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution. Science 268:1758-1762, 1995.
4. 4. Tanaka RD, Edwards PA, Lan SF, Knoppel EM, Fogelman AM. Purification of 3 hydroxy-3-methylglutaryl-coenzyme A reductase from human liver. J Lipid Res 23:523-530, 1982.
5. 5. Chin DJ, Luskey KL, Faust JR, MacDonald RJ, Brown MS, Goldstein JL. Molecular cloning of 3-hydroxy-3-methylglutaryl coenzyme A reductase and evidence for regulation of its mRNA. Proc Natl Acad Sci USA 79: 7704-7708, 1982.
6. 6. Chen GZ, Foster L, Bennett JL. Purification and characterization of 3-hydroxy-3-methylglutaryl-coenzyme A reductase of Schistosoma mansoni: Regulation of parasite enzyme activity differs from mammalian host. Exp Parasitol 73:82-92, 1991.
7. 7. Rogers KS, Hellerman L, Thompson TE. L-Glutamate dehydrogenase. III. Molecular size of bovine glutamate dehydrogenase and the methylmercuric bromide-activated enzyme in the concentration range of enzymatic assay. J Biol Chem 240:198-200, 1965.
8. 8. Darnay BG, Wang Y, Rodwell VW. Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 267:15064-15070, 1992.
9. 9. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem 72:248-254, 1976.
10. 10. Ackers GK. A new calibration procedure for gel filtration columns. J Biol Chem 242:3237, 1967.
11. 11. Valentine RC. The shapes of protein molecules. Proc Eur Reg Conf Electron Microsc Delft 2:708-711, 1960.
12. 12. Himmel ME, Squire PG. Size exclusion parameters. In Aqueous Size-Exclusion Chromatography, Journal of Chromatography Library Series, Vol. 40, (Dubin PL Ed.). Amsterdam: Elsevier, 1988, pp 4-20.
13. 13. Ackers GK. Molecular exclusion and restricted diffusion processes in molecular-sieve chromatography. Biochemistry 3:723-730, 1964.
14. 14. Gosting LJ. Measurement and interpretation of diffusion coefficients of proteins. Adv Protein Chem 11:429-554, 1956.
15. 15. Hansen JC, Lebowitz J, Demeler B. Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 33:13155-13163, 1994.
16. 16. Weast RC, Astel MJ. Handbook of Chemistry and Physics, Vol. 63, Boca Raton, FL: CRC Press, 1983.
17. 17. Creighton TE. Protein, Structure and Molecular Properties. New York: Freeman, 1993.
18. 18. Stata. Statistical Analysis Program. Stata Corp., College Station, TX, 1996.
19. 19. Andrews P. The gel-filtration behavior of proteins related to their molecular weights over a wide range. Biochem J 96:595-605, 1965.
20. 20. Bresnick EH, Felsenfeld G. The leucine zipper is necessary for stabilizing a dimer of the helix-loop-helix transcription factor USF but not for maintenance of an elongated conformation. J Biol Chem 269:21110-21116, 1994.
21. 21. Wu TY, Chang YC. Hydrodynamic and pharmacological characterization of putative α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive L-glutamate receptors solubilized from pig brain. Biochem J 300:365-371, 1994.
22. 22. Chen J, Alberti S, Matthews KS. Wild-type operator binding and altered cooperativity for inducer binding of lac represser dimer mutant r3. J Biol Chem 269:12482-12487, 1994.
23. 23. Xie J, Fleischer B. Isolation and characterization of a novel inositol hexakisphosphate binding protein from mammalian cell cytosol. Biochemistry 33:7908-7916, 1994.
24. 24. Dam TK, Bandyopadhyay P, Sarkar M, Ghosal J, Bhattacharya A, Choudhury A. Purification and partial characterization of a heparin-binding lectin from the marine clam Anadara granosa. Biochem Biophys Res Commun 203:36-45, 1994.
25. 25. Siegel LM, Monty KJ. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim Biophys Acta 112:346-362, 1966.
26. 26. Lawrence CM. The structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 Å resolution. Purdue University, West Lafayette, IN, 1993. [Ph.D. thesis].
27. 27. Bensch WR, Rodwell VW. Purification and properties of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Pseudomonas. J Biol Chem 245:3755-3762, 1970.
28. 28. Gill JF Jr, Beach MJ, Rodwell VW. Mevalonate utilization in Pseudomonas sp. M. Purification and characterization of an inducible 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 260:9393-9398, 1985.
29. 29. Noble CM, Guyer KE, Boots MR, Rogers KS. Molecular weight of bakers yeast β-hydroxy-β-methylglutaryl coenzyme A reductase by molecular sieve chromatography. Enzymologia 40:8-14, 1971.
30. 30. Wang Y, Darnay BG, Rodwell VW. Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 265: 21634-21641, 1990.
31. 31. Sober HA, Harte RA, Sober EK. In Handbook of Biochemistry, Cleveland, OH: CRC Press, 1968, pp C10-C30.
32. 32. Pharmacia. Gel Filtration Theory and Practice. Pharmacia Fine Chemicals, Uppsala, Sweden, 1979.
33. 33. Stryer L. Implications of x-ray crystallographic studies of protein structure. Annu Rev Biochem 37:25-50, 1968.
34. 34. Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff HW, Phillips DC. A three dimensional model of the myoglobin molecule obtained by x-ray analysis. Nature 181:661-663, 1958.
35. 35. Blake LCF, Koenig DF, Mair GA, North ACT, Phillips DC, Sarma VR. Structure of hen-egg white lysozyme. Nature 206:757-761, 1965.
36. 36. Lipscomb WN, Coppola JC, Hartsuck JA, Ludwig ML, Muirhead H, Searl J, Steitz TA. The structure of carboxypeptidase A. III. Molecular structure at 6 Å resolution. J Mol Biol 19:423-441, 1966.
37. 37. Fridborg K, Kannan KK, Litjas A, Laandin J, Standbery B, Standbery R, Tilander B, Wiren G. Crystal structure of human erythrocyte carbonic anhydrase C. III. Molecular structure of the enzyme and one-enzyme-inhibitor complex at 5.5 Å resolution. J Mol Biol 25:505-516, 1967.
38. 38. Perutz MF, Rossmann MG, Callis F, Muirhead H, Will G, North ACT. Structure of haemoglobin. Nature 185:416-427, 1960.
39. 39. Sygusch J, Beaudry D. Preliminary crystallographic investigation of rabbit liver aldolase. J Mol Biol 186:215-217, 1987.
40. 40. Adams MJ, McPherson JA, Rossmann MG, Schevitz RW. The structure of the nicotinamideadenine dinucleotide coenzyme when bound to lactate dehydrogenase. J Mol Biol 51: 31-38, 1970.