{PDOC01028}
{PS01325; LYS_HYDROXYLASE}
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* Lysyl hydroxylase signature *
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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.

-Consensus pattern: P-H-H-D-[SA]-S-T-F
                    [The first H and the D are iron ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 1999 / First entry.

[ 1] 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).
[ 2] 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).
     PubMed=8621606;

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