PROSITE documentation PDOC01028Lysyl hydroxylase signature
Lysyl hydroxylase (EC 1.14.11.4) [1] catalyzes the hydroxylation of lysine residues in X-Lys-Gly sequences in collagens. The resulting hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen crosslinks.
At least three isoforms of the enzyme are known in vertebrates.
The enzyme requires iron, 2-oxoglutarate, oxygen and ascorbate for its activity. Three residues, two histidine and an aspartate, are inolved in the binding of the iron ion [2]. As a signature pattern we selected a conserved region that contains two of these iron-binding ligands.
Last update:July 1999 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kivirikko K.I. Myllylae R. Pihlajaniemi T. |
| Source | (In) Post-translational modifications of proteins, Crabbe M.C., Harding J., Eds., pp 1-51, CRC Press, Boca Raton, (1991). |
| 2 | Authors | Pirskanen A. Kaimio A.M. Myllylae R. Kivirikko K.I. |
| Title | Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. | |
| Source | J. Biol. Chem. 271:9398-9402(1996). | |
| PubMed ID | 8621606 |
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