Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure

Mevarech M, Neumann E (1977)
Biochemistry 16(17): 3786-3792.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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OA
DOI
URN
urn:nbn:de:0070-pub-17744180
Autor*in
Mevarech, Moshe; Neumann, EberhardUniBi
Einrichtung
Fakultät für Chemie
Stichworte
Molecular biology; Biochemistry
Erscheinungsjahr
1977
Zeitschriftentitel
Biochemistry
Band
16
Ausgabe
17
Seite(n)
3786-3792
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1774418

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Mevarech M, Neumann E. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry. 1977;16(17):3786-3792.
Mevarech, M., & Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry, 16(17), 3786-3792. https://doi.org/10.1021/bi00636a010
Mevarech, Moshe, and Neumann, Eberhard. 1977. “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure”. Biochemistry 16 (17): 3786-3792.
Mevarech, M., and Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry 16, 3786-3792.
Mevarech, M., & Neumann, E., 1977. Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry, 16(17), p 3786-3792.
M. Mevarech and E. Neumann, “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure”, Biochemistry, vol. 16, 1977, pp. 3786-3792.
Mevarech, M., Neumann, E.: Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure. Biochemistry. 16, 3786-3792 (1977).
Mevarech, Moshe, and Neumann, Eberhard. “Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 2. Effect of salt on the catalytic activity and structure”. Biochemistry 16.17 (1977): 3786-3792.
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19 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Hydration shells with a pinch of salt.
Zaccai G., Biopolymers 99(4), 2013
PMID: 23348670
Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein.
Madern D, Zaccai G., Biochimie 86(4-5), 2004
PMID: 15194233
Genes from Debaryomyces hansenii increase salt tolerance in Saccharomyces cerevisiae W303.
Prista C, Soeiro A, Vesely P, Almagro A, Ramos J, Loureiro-Dias MC., FEMS Yeast Res 2(2), 2002
PMID: 12702302
Halophilic enzymes: proteins with a grain of salt.
Mevarech M, Frolow F, Gloss LM., Biophys Chem 86(2-3), 2000
PMID: 11026680
Expression of Batis maritima methyl chloride transferase in Escherichia coli.
Ni X, Hager LP., Proc Natl Acad Sci U S A 96(7), 1999
PMID: 10097085
Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts.
Madern D, Pfister C, Zaccai G., Eur J Biochem 230(3), 1995
PMID: 7601139
Further thermal characterization of an aspartate aminotransferase from a halophilic organism.
Muriana FJ, Alvarez-Ossorio MC, Relimpio AM., Biochem J 298 ( Pt 2)(), 1994
PMID: 8135756
Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri.
Breitung J, Börner G, Scholz S, Linder D, Stetter KO, Thauer RK., Eur J Biochem 210(3), 1992
PMID: 1483480
Halophilic proteins and the influence of solvent on protein stabilization.
Zaccai G, Eisenberg H., Trends Biochem Sci 15(9), 1990
PMID: 2238041
Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity.
Hecht K, Wrba A, Jaenicke R., Eur J Biochem 183(1), 1989
PMID: 2753046
Stabilization of halophilic malate dehydrogenase.
Zaccai G, Cendrin F, Haik Y, Borochov N, Eisenberg H., J Mol Biol 208(3), 1989
PMID: 2795658
Polypeptide elongation factor Tu from Halobacterium marismortui.
Guinet F, Frank R, Leberman R., Eur J Biochem 172(3), 1988
PMID: 3127212
Crystallization of halophilic malate dehydrogenase from Halobacterium marismortui.
Harel M, Shoham M, Frolow F, Eisenberg H, Mevarech M, Yonath A, Sussman JL., J Mol Biol 200(3), 1988
PMID: 3398050
Methanogens and the diversity of archaebacteria.
Jones WJ, Nagle DP, Whitman WB., Microbiol Rev 51(1), 1987
PMID: 3104748
Solution structure of halophilic malate dehydrogenase from small-angle neutron and X-ray scattering and ultracentrifugation.
Zaccai G, Wachtel E, Eisenberg H., J Mol Biol 190(1), 1986
PMID: 3783699
Effect of Cl- on the function of the Cl- -activated arginine aminopeptidase purified from human erythrocytes.
Söderling E., Arch Biochem Biophys 216(1), 1982
PMID: 7103502
Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration.
Pundak S, Eisenberg H., Eur J Biochem 118(3), 1981
PMID: 7297556
Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability.
Pundak S, Aloni H, Eisenberg H., Eur J Biochem 118(3), 1981
PMID: 7297557
A comparative study on the stability of immobilized halophilic and non-halophilic malate dehydrogenases at various ionic strengths.
Koch-Schmidt AC, Mosbach K, Werber MM., Eur J Biochem 100(1), 1979
PMID: 488091

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