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UDP-glucuronate carboxy-lyase has been demonstrated in chick chondrocytes in tissue culture. It occurs in the particulate fraction, and its activity is stimulated by exogenous NAD. The enzyme is allosterically activated by UDP-glucuronate and inhibited by UDP-xylose, n Values of 2.8 indicate positive cooperativity of at least three interacting sites on the enzyme. These data suggest that UDP-xylose concentration in chondrocytes is regulated by substrate activation and product inhibition of UDP-glucuronate carboxy-lyase. Activity levels of the enzyme during growth of the cells peak towards mid-log phase and decline thereafter, closely paralleling levels of chondroitin sulfate glycosyltransferases determined previously (Schwartz, N. B. (1976) J. Biol. Chem. 251, 3346-3351). Thus, it appears that during chondrocyte development a common mechanism governs induction of glycosyltransferases and of UDP-glucuronate carboxy-lyase.
K V John, and
N B Schwartz, and
H Ankel
November 1977,
The Journal of biological chemistry,
K V John, and
N B Schwartz, and
H Ankel
November 2002,
Plant & cell physiology,
K V John, and
N B Schwartz, and
H Ankel
February 1972,
Archives of biochemistry and biophysics,
K V John, and
N B Schwartz, and
H Ankel
January 1966,
Biochemistry,
K V John, and
N B Schwartz, and
H Ankel
April 2006,
The FEBS journal,
K V John, and
N B Schwartz, and
H Ankel
April 1969,
Biochimica et biophysica acta,
K V John, and
N B Schwartz, and
H Ankel
May 2023,
Nature communications,
K V John, and
N B Schwartz, and
H Ankel
November 1982,
Journal of bacteriology,
K V John, and
N B Schwartz, and
H Ankel
October 1990,
Biochemical Society transactions,
K V John, and
N B Schwartz, and
H Ankel
February 1963,
Biochimica et biophysica acta,
