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Effects of solubilisation on some properties of the membrane‐bound respiratory enzyme D‐amino acid dehydrogenase of Escherichia coli
Author(s) -
Jones H.,
Venables W.A.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80066-0
Subject(s) - enzyme , chemistry , substrate (aquarium) , escherichia coli , dehydrogenase , biochemistry , membrane , denaturation (fissile materials) , chromatography , amino acid , biology , nuclear chemistry , ecology , gene
Solubilisation, delipidation and partial purification of the membrane‐bound enzyme. D‐amino acid dehydrogenase of Escherichia coli K 12 produced significant changes in several of its properties. Solubilised enzyme showed a broader substrate specificity, increased affinity for at least three substrates, and a lower pH optimum with D‐alanine as substrate. Solubilised enzyme was more heat‐labile than native enzyme, particularly at 37°C, and re‐binding to envelope preparations restored protection against heat denaturation. Activity of delipidated enzyme could be increased by addition of pure phospholipids. Native enzyme showed biphasic Arrhenius kinetics associated with phase changes of membrane lipids.