prolyl hydroxylase

(redirected from Prolyl 4-hydroxylase)
Also found in: Acronyms.

pro·lyl hy·drox·y·lase

an enzyme that catalyzes the hydroxylation of certain prolyl residues in collagen precursors using molecular oxygen, ferrous ion, ascorbic acid, and α-ketoglutarate; a vitamin C deficiency directly affects the activity of this enzyme; one form of this enzyme (prolyl 4-hydroxylase) synthesizes 4-hydroxyprolyl residues while another produces 3-hydroxyprolyl residues.
Mentioned in ?
References in periodicals archive ?
Kivirikko, "The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells," The Journal of Biological Chemistry, vol.
Pickering, "Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque," Circulation, vol.
As mentioned above prolyl 4-hydroxylase is needed to produce stable collagen protein, so in this project we had to construct two additional vectors containing expression cassette of [alpha] and [beta] genes of prolyl 4-hydroxylase.
Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase.
Coexpression with collagen markedly increases the half-life of the recombinant human prolyl 4-hydroxylase tetramer in the yeast Pichia pastoris.
Prolyl 4-hydroxylase catalyzes the hydroxylation of proline residues in repeating X-Pro-Gly triplets, thus forming the 4-hydroxyproline required for the correct folding of newly synthesized collagen (Kivirikko and Myllyharju, 1998; Kivirikko and Pihlajaniemi, 1998; Myllyharju, 2003).
Regulation of the amount of active prolyl 4-hydroxylase tetramer appears to be linked to synthesis of the [alpha]-subunit (Kivirkko et al., 1992).
mRNA levels for [alpha]-subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle.
Molecular cloning of the [alpha]-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts.
Structural requirements for the utilization of ascorbate analogues in the prolyl 4-hydroxylase reaction.
Inhibition by N-oxalylamino acid derivatives, first developed for use with collagen prolyl 4-hydroxylases, further implies that these hydroxylases are also dependent upon 2OG as a cosubstrate (Cunliffe et al.
Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor.