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Conservation from rat to human of cytosolic phospho enol pyruvate carboxykinase and the control of its gene expression
Author(s) -
Cohen Hannah,
Gidoni Bruriah,
Shouval Daniel,
Benvenisty Nissim,
Mencher David,
Meyuhas Oded,
Reshef Lea
Publication year - 1985
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(85)81066-8
Subject(s) - cytosol , isozyme , biochemistry , biology , pyruvate dehydrogenase complex , enol , chemistry , enzyme , microbiology and biotechnology , catalysis
Structural conservation of cytosolic phospho enol pyruvate carboxykinase protein and mRNA sequence was found in all species examined from rodents to human. The mitochondrial isoenzyme, in all species tested, represents a distinct protein. Moreover, irrespective of the ratio of cytosolic to mitochondrial isoenzyme, cytosolic phospho enol pyruvate carboxykinase activity in the human as in the rat is controlled at the level of gene expression and through the same multiple hormonal stimulation. This evolutionary conservation of the cytosolic phospho enol pyruvate carboxykinase structure and mode of regulation supports the enzymes' physiological importance in mammals.