Lysyl hydroxylases
| PLOD1 | ||
|---|---|---|
| other names |
Procollagen lysines, 2-oxoglutarate 5-dioxygenase 1; LLH; LH1; Lysyl hydroxylase 1; EC 1.14.11.4; PLOD; EDS6; Procollagen-Lysine 1, 2-Oxoglutarate 5-Dioxygenase (Lysine Hydroxylase, Ehlers-Danlos Syndrome Type VI); Procollagen lysines 1, 2-oxoglutarate 5-dioxygenase 1; Procollagen lysines, 2-oxoglutarate 5-dioxygenase 1; Lysyl hydroxylase 1; Lysine hydroxylase; LH |
|
| Properties of human protein | ||
| Mass / length primary structure | 727 amino acids, 83550 Da | |
| Identifier | ||
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 5351 | 18822 |
| UniProt | Q02809 | Q9R0E2 |
| PubMed search | 5351 |
18822
|
The lysyl hydroxylases are enzymes that catalyze the hydroxylation of lysine residues in proteins .
The Lysylhydroxylasen produce lysine residues of hydroxylysine as post-translational modification , including in the stabilization of collagen . Cofactors are iron ions and ascorbic acid (vitamin C). Lysyl hydroxylases are dimers and localized in the lumen of the rough endoplasmic reticulum . A deficiency in vitamin C leads to defects in the function of collagen, which are counted among the symptoms of scurvy .
literature
- Jeremy M. Berg, John L. Tymoczko, Lubert Stryer : Biochemistry. 6th edition, Spektrum Akademischer Verlag, Heidelberg 2007, ISBN 978-3-8274-1800-5 .
- Donald Voet, Judith G. Voet: Biochemistry. 3rd edition, John Wiley & Sons, New York 2004, ISBN 0-471-19350-X .
- Bruce Alberts , Alexander Johnson, Peter Walter, Julian Lewis, Martin Raff, Keith Roberts: Molecular Biology of the Cell . 5th edition, Taylor & Francis 2007, ISBN 978-0-8153-4106-2 .
Individual evidence
- ↑ Jari Heikkinen, Maija Risteli, Outi Lampela, Paula Alavesa, Marjo Karppinen, André H. Juffer, Raili Myllylä: Dimerization of human lysyl hydroxylase 3 (LH3) is mediated by the amino acids 541-547 . In: Matrix Biology . tape 30 , no. 1 , January 2011, p. 27-33 , doi : 10.1016 / j.matbio.2010.10.002 , PMID 20955792 .