Home | Contact

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.

July 1999 / First entry.

PROSITE method (with tools and information) covered by this documentation:

LYS_HYDROXYLASE, PS01325; Lysyl hydroxylase signature  (PATTERN)

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

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01325 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01325 • Scan Swiss-Prot/TrEMBL entries against PS01325 • view ligand binding statistics

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

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)

SIB Swiss Institute of Bioinformatics | Disclaimer