The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction
Abstract
In the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by prolyl 4-hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) is stoicheiometrically coupled to the oxidation of ascorbate. The Km and Kd for O2 in this partial reaction are 1.5 mM, this value being one order of magnitude higher than the Km and Kd for O2 in the complete reaction in the presence of (Pro-Pro-Gly)5, indicating that in this case O2 can become enzyme-bound predominantly after the interaction of the peptide substrate with the enzyme. The Km values for 2-oxoglutarate in the partial and the complete reactions are the same. In the absence of both a peptide substrate and ascorbate 2 mol CO2 per mol enzyme are produced in the first 1-1.5 min, during which the enzyme becomes inactivated and, as shown earlier (De Jong , L., Albracht , S.P.J. and Kemp, A. (1982) Biochim. Biophys. Acta 704, 326-332) enzyme-bound Fe2+ becomes oxidized to Fe3+. The results are consistent with a mechanism in which a Fe2+O complex is the O-transferring intermediate involved in peptidylproline hydroxylation.
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“Ascorbate, which is also known as vitamin C (VitCred), rescues the enzyme by reducing the inactive Fe(III) state to the active Fe(II) state.10,11”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [11]
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Cites
The role of ascorbate in the prolyl hydroxylase reaction
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Cited by
Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937
Tissue oxygenation, anemia, and perfusion in relation to wound healing in surgical patients.
JONSSON, K., JENSEN, J. A., GOODSON, W. H., SCHEUENSTUHL, H., WEST, J., HOPF, H. W., & HUNT, T. K. (1991) · Annals of Surgery · doi:10.1097/00000658-199111000-00011 · Cited by 462
Kivirikko, K. I., Myllylä, R., & Pihlajaniemi, T. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.5.2537773 · Cited by 320
Koivunen, P., Hirsilä, M., Kivirikko, K. I., & Myllyharju, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604628200 · Cited by 129
Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center
Vasta, J. D., & Raines, R. T. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00251 · Cited by 36
Metadata
- Authors
- Jong, L. D., & Kemp, A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 1984-05
- Volume
- 787
- Issue
- 1
- Pages
- 105-111
- ISSN
- 0167-4838
- Cited by
- 65
- References
- 1
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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