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Cited by 200

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase.

Myllylä, R, Majamaa, K, Günzler, V, Hanauske-Abel, H M, Kivirikko, K I·1984·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)91023-9
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Abstract

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.

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1 of 1 references verified0 citation errors · 0 not checkable

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Citations

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Show all 1 references

Research works printed but not linked: 19

  1. Cardinale, 1974, Adv. Enzymol., 41, 245
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Cited by

Metadata

Authors
Myllylä, R., Majamaa, K., Günzler, V, Hanauske-Abel, H. M., & Kivirikko, K. I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1984-05
Volume
259
Issue
9
Pages
5403-5405
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)91023-9
Cited by
200
References
1
Language
en
Licence

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