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Distinct physiological roles of animal succinate thiokinases Association of guanine nucleotide‐linked succinate thiokinase with ketone body utilization
Author(s) -
Jenkins T.M.,
Weitzman P.D.J.
Publication year - 1986
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(86)80900-0
Subject(s) - nucleotide , guanine , ketone bodies , biochemistry , gtp' , enzyme , citric acid cycle , adenine nucleotide , chemistry , biology , metabolism , gene
Two distinct succinate thiokinases have recently been shown to exist in animal tissues, one specific for guanine nucleotide and the other for adenine nucleotide. Their physiological roles have here been investigated by comparing the levels of the two enzymes in liver and brain of normal and diabetic rats. A marked rise in the level of brain guanine nucleotide‐linked succinate thiokinase in the diabetic condition is consistent with an enhanced utilization of ketone bodies and hence with the associated elevated demand for succinyl‐CoA for the activation of acetoacetate. Taken together with the reported mitochondrial values of the ATP/ADP and GTP/GDP ratios, the results are interpreted to indicate that the adenine nucleotide‐linked enzyme functions as a component of the citric add cycle whereas the guanine nucleotide‐linked enzyme functions in the opposite metabolic direction to produce succinyl‐CoA from succinate.