|PROSITE documentation PDOC01028
Lysyl hydroxylase signature
Lysyl hydroxylase (EC 184.108.40.206)  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 . As a signature pattern we selected a conserved
region that contains two of these iron-binding ligands.
July 1999 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|LYS_HYDROXYLASE, PS01325; Lysyl hydroxylase signature (PATTERN)
The first H and the D are iron ligands
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
||Kivirikko K.I., Myllylae R., Pihlajaniemi T.
||(In) Post-translational modifications of proteins, Crabbe M.C., Harding J., Eds., pp 1-51, CRC Press, Boca Raton, (1991).
||Pirskanen A., Kaimio A.M., Myllylae R., Kivirikko K.I.
||Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity.
||J. Biol. Chem. 271:9398-9402(1996).
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