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Prolyl 4-hydroxylase

Gorres, Kelly L., Raines, Ronald T.·2010·Critical Reviews in Biochemistry and Molecular Biology
DOI 10.3109/10409231003627991PMC PMC2841224
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Abstract

Posttranslational modifications can cause profound changes in protein function. Typically, these modifications are reversible, and thus provide a biochemical on-off switch. In contrast, proline residues are the substrates for an irreversible reaction that is the most common posttranslational modification in humans. This reaction, which is catalyzed by prolyl 4-hydroxylase (P4H), yields (2S,4R)-4-hydroxyproline (Hyp). The protein substrates for P4Hs are diverse. Likewise, the biological consequences of prolyl hydroxylation vary widely, and include altering protein conformation and protein-protein interactions, and enabling further modification. The best known role for Hyp is in stabilizing the collagen triple helix. Hyp is also found in proteins with collagen-like domains, as well as elastin, conotoxins, and argonaute 2. A prolyl hydroxylase domain protein acts on the hypoxia inducible factor alpha, which plays a key role in sensing molecular oxygen, and could act on inhibitory kappaB kinase and RNA polymerase II. P4Hs are not unique to animals, being found in plants and microbes as well. Here, we review the enzymic catalysts of prolyl hydroxylation, along with the chemical and biochemical consequences of this subtle but abundant posttranslational modification.

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Metadata

Authors
Gorres, K. L., & Raines, R. T.
Venue
Critical Reviews in Biochemistry and Molecular Biology
Publisher
Informa UK Limited
Published
2010-03-04
Volume
45
Issue
2
Pages
106-124
ISSN
  • 1040-9238
  • 1549-7798
DOI
10.3109/10409231003627991
PMC
PMC2841224
Cited by
591
References
9
Language
en

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Gorres, K. L., & Raines, R. T. (2010). Prolyl 4-hydroxylase. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.3109/10409231003627991

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