Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus

Archives of Microbiology

Volumn 168, Issue 1, 1997, Pages 59-67

  Langelandsvik, Anne Siri ^a   Steen, Ida Helene ^a,b   Birkeland, Nils Kåre ^a   Lien, Torleiv ^a  

^a UNIVERSITY OF BERGEN   (Norway)

^b UNIVERSITY OF BERGEN   (Norway)

Author keywords

Archaea; Archaeoglobus fulgidus; Glycine motif; Lactate dehydrogenase; Lactate dehydrogenase like malate dehydrogenase; Malate dehydrogenase; Mdh; Thermophiles; Thermostable protein

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; DIPOTASSIUM HYDROGEN PHOSPHATE; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; OXALOACETIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARCHAEOGLOBUS FULGIDUS; ARTICLE; CATALYSIS; CONTROLLED STUDY; DNA SEQUENCE; ENZYME ISOLATION; ENZYME PURIFICATION; ISOELECTRIC POINT; MOLECULAR WEIGHT; NONHUMAN; PHYLOGENY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; ARCHAEA; BASE SEQUENCE; CLONING, MOLECULAR; HEATING; MALATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; NAD; OXALOACETATES; OXALOACETIC ACIDS; PHOSPHATES; PHYLOGENY; POTASSIUM COMPOUNDS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; ARCHAEOGLOBUS FULGIDUS; BACTERIA (MICROORGANISMS); HALOARCULA MARISMORTUI; POSIBACTERIA; THERMOTOGA MARITIMA;

EID: 0030829444     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050470     Document Type: Article

References (53)

1. Alldread RM, Halsall DM, Clarke AR, Sundaram TK, Atkinson T, Scawen MD, Nicholls DJ (1995) Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding. Biochem J 305:539-548
2. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403-410
3. Birktoft JJ, Banaszak LJ (1983) The presence of a histidine-aspartic acid pair in the active site of 2-hydroxy acid dehydrogenases. J Biol Chem 258:472-482
4. Birktoft JJ, Banaszak LJ (1984) Structure-function relationships among nicotinamide-adenine dinucleotide dependent oxidoreductases. Pept Protein Rev 4:1-46
5. Birktoft JJ, Fernley RT, Bradshaw RA, Banaszak LJ (1982) Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenase form a homologous system with lactate dehydrogenase. Proc Natl Acad Sci USA 79:6166-6170
6. Birktoft JJ, Rhodes G, Banaszak LJ (1989) Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution. Biochemistry 28:6065-6081
7. Boernke WE, Millard CS, Stevens PW, Kakar SN, Stevens FJ, Donnelly MI (1995) Stringency of substrate specificity of Escherichia coli malate dehydrogenase. Arch Biochem Biophys 322:43-53
8. Bradford MM (1976) Rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
9. M) and thermostability in the presence of salts. Arch Microbiol 156:517-524
10. Breitung J, Borner G, Scholz S, Linder D, Stetter KO, Thauer RK (1992) Salt dependence, kinetic properties and catalytic mechanism of the N-formylmethanofuran: tetrahydro-methanopterin formyltranseferase from the extreme thermophile Methanopyrus kandleri. Eur J Biochem 210:971-981
11. Bult CJ, While O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG, Blake JA, FitzGerald LM, Clayton RA, Gocayne JD, Kerlavage AR, Dougherty BA, Tomb J-F, Adams MD, Reich CI, Overbeek R, Kirkness EF, Weinstock KG, Merrick JM, Glodek A, Scott JL, Geoghagen NSM, Weidman JF, Fuhrmann JL, Nguyen D, Utterback TR, Kelly JM, Peterson JD, Sadow PW, Hanna MC, Cotton MD, Roberts KM, Hurst MA, Kaine BP, Borodovsky M, Klenk H-P, Fraser CM, Smith HO, Woese CR, Venter JC (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1017-1140
12. Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M (1993) Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32:4308-4313
13. Charnock C, Refseth UH, Sirevåg R (1992) Malate dehydrogenase from Chlorobium vibrioforme. Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis. J Bacteriol 174:1307-1313
14. Clarke AR, Wigley DB, Chia WN, Barstow D, Atkinson T, Holbrook JJ (1986) Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis. Nature 324:699-702
15. Dahl C, Kredich NM, Deutzmann R, Trüper HG (1993) Dissimilatory sulphite reductase from Archacoglobus fulgidus: physicochemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes. J Gen Microbiol 139:1817-1828
16. Dalgaard JZ, Garret RA (1993) Archaeal hyperthermophile genes. In: Kates M, Kushner DJ, Matheson AT (eds) The biochemistry of the Archaea. Elsevier, Amsterdam, pp 535-563
17. Danson MJ (1993) Central metabolism of the archaea. In: Kates M, Kushner DJ, Matheson AT (eds) The biochemistry of the Archaea. Elsevier, Amsterdam, pp 1-24
18. Eventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH (1977) Structural adaptations of lactate dehydrogenase isozymes. Proc Natl Acad Sci USA 74:2677-2681
19. Grossebüter W, Hartl T, Görisch H, Stezowski JJ (1986) Purification and properties of malate dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biol Chem Hoppe Seyler 367:457-463
20. Hall MD, Levitt DG, Banaszak LJ (1992) Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 Å resolution. J Mol Biol 226: 867-882
21. Hart KW, Clarke AR, Wigley DB, Chia WN, Barstow DA, Atkinson T, Holbrook JJ (1987) The importance of arginine-171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase. Biochem Biophys Res Commun 146:346-353
22. Hartl T, Grossebüter W, Görisch H, Stezowski JJ (1987) Crystalline NAD/NADP-dependent malate dehydrogenase: the enzyme from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biol Chem Hoppe Seyler 368:259-267
23. Hensel R (1993). Proteins of extreme thermophiles. In: Kates M, Kushner DJ, Matheson AT (eds) The biochemistry of the Archaea. Elsevier, Amsterdam, pp 209-221
24. Hensel R, König H (1988) Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol Lett 49:75-79
25. Honka E, Fabry S, Niermann T, Palm P, Hensel R (1990) Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur J Biochem 188:623-632
26. Iijima S, Takashi S, Beppu T (1980) Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermits flavus AT-62. Biochim Biophys Acta 613:1-9
27. Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ (1993) Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry 32:3913-3922
28. 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
29. 420-dependent NADP reductase in the extremely thermophilic sulfate-reducing Archaeoglobus fulgidus. Arch Microbiol 160: 199-205
30. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
31. Mevarech M, Leicht W, Werber MM (1976) Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate. Biochemistry 15:2383-2386
32. Mevarech M, Eisenberg H, Neumann E (1977) Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. I. Purification and molecular characterization. Biochemistry 16:3781-3785
33. 420 in Archaeoglobus fulgidus. Arch Microbiol 152:362-368
34. Muir JM, Russell RJM, Hough DW, Danson MJ (1995) Citrate synthase from the hyperthermophilic archaeon, Pyrococcus furiosus. Protein Eng 8:583-592
35. Nicholls DJ, Miller J, Scawen MD, Clarke AR, Holbrook JJ, Atkinson T, Goward CR (1992) The importance of arginine-102 for the substrate specificity of Escherichia coli malate dehydrogenase. Biochem Biophys Res Commun 189:1057-1062
36. Novotny JF, Perry JJ (1990) Characterization of the malate dehydrogenase from Thermoleophilum album NM. Arch Microbiol 154:304-307
37. Reiter W, Palm P, Zillig W (1988) Transcription termination in the archaebacterium Sulfolobus: signal structures and linkage to transcription initiation. Nucleic Acids Res 16:2445-2459
38. Rossmann MG, Moras D, Olsen KW (1974) Chemical and biological evolution of a nucleotide-binding protein. Nature 250:194-199
39. Russell RJM, Taylor GL (1995) Engineering thermostability: lessons from thermophilic proteins. Curr Opin Biotechnol 6: 370-374
40. Sambrook JE, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
41. Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463-5467
42. 10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea. Arch Microbiol 159:225-232
43. Sprott GD, McKellar RC, Shaw KM, Giroux J, Martin WG (1979) Properties of malate dehydrogenase isolated from Methanospirillum hungatii. Can J Microbiol 25:192-200
44. Stetter KO (1988) Archaeoglobus fulgidus gen. nov., sp. nov.: a new taxon of extremely thermophilic archaebacteria. Syst Appl Microbiol 10:172-173
45. Sundaram TK, Wright IP, Wilkinson AE (1980) Malate dehydrogenase from thermophilic and mesophilic bacteria. Molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity. Biochemistry 19:2017-2022
46. Thomm M (1996) Archaeal transcription factors and their role in transcription initiation. FEMS Microbiol Rev 18:159-171
47. Widdel F, Pfennig N (1984) Dissimilatory sulfate- or sulfur-reducing bacteria. In: Krieg NR, Holt JG (eds) Bergey's manual of systematic bacteriology, vol 1. Williams & Wilkins, Baltimore, pp 663-679
48. Wierenga RK, Hol WGJ (1983) Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant. Nature 302:842-844
49. Wierenga RK, Terpstra P, Hol WGJ (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins using an amino acid sequence fingerprint. J Mol Biol 187:101-107
50. Wilks HM, Hart KW, Feeney R, Dunn CR, Muirhead H, Chia WN, Barstow DA, Atkinson T, Clarke AR, Holbrook JJ (1988) A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science 242:1541-1544
51. Yip KSP, Stillman TJ, Britton KL, Artymiuk PJ, Baker 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
52. Yueh AY, Chung CS, Lai YK (1989) Purification and molecular properties of malate dehydrogenase from the marine diatom Nitschia alba. Biochem J 258:221-228
53. Zillig W, Palm P, Klenk H, Langer D, Hüdepohl U, Hain J, Lanzendörfer M, Holz I (1993) Transcription in arcahea. In: Kates M, Kushner DJ, Matheson AT (eds) The biochemistry of the Archaea. Elsevier, Amsterdam, pp 367-391