Characterization of an essential histidine residue in thermophilic malate dehydrogenase.

Abstract:

:Heat-stable malate dehydrogenase isolated from Thermus flavus AT62 was completely inactivated by treatment with diethylpyrocarbonate. The inactivation was accompanied by the loss of 1.2 histidine residues per subunit of the enzyme. The enzyme was protected from inactivation by NADH. The enzyme was also inactivated by dye-sensitized photooxidation. Methionine residues, in addition to histidine residues, were destroyed in the inactivated enzyme. Kinetic analyses of the inactivation indicated that the pK value of the residue involved in the inactivation was 8.20 at 25.0 degrees C and 7.52 at 60.0 degrees C. From the pK values and the heat of ionization calculated from the van't Hoff plot of pKs, a histidine residue was identified to be primarily involved in the inactivation. The effect of temperature on the pK value of the essential group in this enzyme from a thermophilic organism is discussed.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Iijima S,Oh MJ,Saiki T,Beppu T

doi

10.1093/oxfordjournals.jbchem.a135641

subject

Has Abstract

pub_date

1986-06-01 00:00:00

pages

1667-72

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

99

pub_type

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