lysyl hydroxylase

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ly·syl hy·drox·y·lase

an enzyme that acts on specific lysyl residues in certain proteins (for example, collagens) with α-ketoglutarate and O2 to produce δ-hydroxylysyl residues, succinate, and CO2; this enzyme, which requires Fe2+ and ascorbate, is deficient in Ehlers-Danlos syndrome type VI.
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References in periodicals archive ?
Vapola et al., "Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes," Journal of Cell Science, vol.
Kivirikko, and R.Myllyla, "Cloning of human lysyl hydroxylase: Complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3 [right arrow] p36.2," Genomics, vol.
Yeowell, "Fox-2 protein regulates the alternative splicing of scleroderma-associated lysyl hydroxylase 2 messenger RNA," Arthritis and Rheumatism, vol.
Interestingly, VitC-dependent collagen prolyl and lysyl hydroxylases are key regulators of breast cancer metastasis [79, 96, 97].
Mutations in the lysyl hydroxylase 1 gene that result in enzyme deficiency and the clinical phenotype of Ehlers-Danlos syndrome type VI.
A homozygous stop codon in the lysyl hydroxylase gene in two siblings with Ehlers-Danlos syndrome type VI.
The hydroxylation is catalyzed by a variety of nonheme iron-containing dioxygenases, including prolyl, asparaginyl, and lysyl hydroxylases (Hewitson et al.