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J. Biol. Chem., Vol. 259, Issue 9, 5403-5405, 05, 1984
R Myllyla, K Majamaa, V Gunzler, HM Hanauske-Abel and KI Kivirikko
The hydroxylation of proline and lysine residues by the collagen
hydroxylases is coupled with a stoichiometric decarboxylation of 2-
oxoglutarate. Ascorbate is virtually a specific requirement for these
enzymes, but previous studies have demonstrated that it is not consumed
during most catalytic cycles. Prolyl 4-hydroxylase and lysyl hydroxylase
are known also to catalyze an uncoupled decarboxylation of 2-oxoglutarate
in the absence of the peptide substrate. It is shown here that, unlike the
complete hydroxylation reaction, the uncoupled decarboxylation reaction
involves stoichiometric ascorbate consumption. This stoichiometric
ascorbate consumption was also seen when the rate of the uncoupled prolyl
4-hydroxylase reaction was enhanced by the addition of poly(L-proline).
Since collagen hydroxylases may catalyze occasional uncoupled reaction
cycles even in the presence of the peptide substrates, the main function of
ascorbate in these reactions in vivo is suggested to be that of
reactivating the enzymes after such uncoupled cycles.
Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
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