Lysyl hydroxylase: Difference between revisions
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{{protein | {{infobox protein | ||
| Name = procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase 1 | | Name = procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase 1 | ||
| caption = | | caption = | ||
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| LocusSupplementaryData = -36.2 | | LocusSupplementaryData = -36.2 | ||
}} | }} | ||
{{protein | {{infobox protein | ||
| Name = procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 | | Name = procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 | ||
| caption = | | caption = | ||
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| LocusSupplementaryData = | | LocusSupplementaryData = | ||
}} | }} | ||
'''Lysyl hydroxylases''' (or '''procollagen-lysine 5-dioxygenases''') are [[2-oxoglutarate (2OG)-dependent dioxygenases | 2-oxoglutarate (2OG)-dependent dioxygenase]] [[enzyme]]<nowiki/>s that catalyze the [[hydroxylation]] of [[lysine]] to [[hydroxylysine]].<ref>{{cite journal | vauthors = Hausmann E | title = Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen | journal = Biochimica et Biophysica Acta | volume = 133 | issue = 3 | pages = 591–3 | date = Apr 1967 | pmid = 6033801 | doi = 10.1016/0005-2795(67)90566-1 }}</ref><ref>{{cite journal | vauthors = Rhoads RE, Udenfriend S | title = Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 60 | issue = 4 | pages = 1473–8 | date = Aug 1968 | pmid = 5244754 | pmc = 224943 | doi = 10.1073/pnas.60.4.1473 }}</ref> Lysyl hydroxylases require [[iron]] and [[vitamin C]] as [[cofactor (biochemistry)|cofactors]] for their oxidation activity. It takes place (as a [[post-translational modification]]) following collagen synthesis in the cisternae (lumen) of the [[rough endoplasmic reticulum|rough endoplasmic reticulum (ER)]]. There are three lysyl hydroxylases (LH1-3) encoded in the human genome, namely: ''PLOD1'', ''PLOD2'' and ''PLOD3''. From ''PLOD2'' two splice variant can be expressed (LH2a and LH2b), where LH2b differs from LH2a by incorporating the small exon 13A. LH1 and LH3 hydroxylate lysyl residues in the collagen triple helix, whereas LH2b hydroxylates lysyl residues in the telopeptides of collagen. In addition to its hydroxylation activity, LH3 has glycosylation activity that produces either monosaccharide (Gal) or disaccharide (Glc-Gal) attached to collagen hydroxylysines. | |||
Collagen lysyl hydroxylation is the first step in collagen [[pyridinoline]] cross-linking, that is necessary for the stabilization of [[collagen]]. | |||
== | ==Pathology== | ||
'' | Mutations in the ''PLOD2'' gene have been linked to [[Bruck syndrome]] in humans. | ||
A deficiency in its cofactor, vitamin C, is associated with [[scurvy]]. | |||
== | == References == | ||
{{reflist}} | |||
==External links== | == External links == | ||
* {{MeshName|Lysyl+Hydroxylase}} | * {{MeshName|Lysyl+Hydroxylase}} | ||
{{Amino acid metabolism enzymes}} | |||
{{Fibrous proteins}} | |||
{{Dioxygenases}} | |||
{{Enzymes}} | |||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
[[Category:Human 2OG oxygenases]] | |||
[[Category:EC 1.14.11]] | |||
[[Category:Extracellular matrix remodeling enzymes]] | |||
{{ | {{oxidoreductase-stub}} | ||
Revision as of 09:41, 23 November 2017
| procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase 1 | |
|---|---|
| Identifiers | |
| Symbol | PLOD1 |
| Alt. symbols | LLH, PLOD |
| Entrez | 5351 |
| HUGO | 9081 |
| OMIM | 153454 |
| RefSeq | NM_000302 |
| UniProt | Q02809 |
| Other data | |
| EC number | 1.14.11.4 |
| Locus | Chr. 1 p36.3-36.2 |
| procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 | |
|---|---|
| Identifiers | |
| Symbol | PLOD2 |
| Entrez | 5352 |
| HUGO | 9082 |
| OMIM | 601865 |
| RefSeq | NM_000935 |
| UniProt | O00469 |
| Other data | |
| Locus | Chr. 3 q24 |
Lysyl hydroxylases (or procollagen-lysine 5-dioxygenases) are 2-oxoglutarate (2OG)-dependent dioxygenase enzymes that catalyze the hydroxylation of lysine to hydroxylysine.[1][2] Lysyl hydroxylases require iron and vitamin C as cofactors for their oxidation activity. It takes place (as a post-translational modification) following collagen synthesis in the cisternae (lumen) of the rough endoplasmic reticulum (ER). There are three lysyl hydroxylases (LH1-3) encoded in the human genome, namely: PLOD1, PLOD2 and PLOD3. From PLOD2 two splice variant can be expressed (LH2a and LH2b), where LH2b differs from LH2a by incorporating the small exon 13A. LH1 and LH3 hydroxylate lysyl residues in the collagen triple helix, whereas LH2b hydroxylates lysyl residues in the telopeptides of collagen. In addition to its hydroxylation activity, LH3 has glycosylation activity that produces either monosaccharide (Gal) or disaccharide (Glc-Gal) attached to collagen hydroxylysines.
Collagen lysyl hydroxylation is the first step in collagen pyridinoline cross-linking, that is necessary for the stabilization of collagen.
Pathology
Mutations in the PLOD2 gene have been linked to Bruck syndrome in humans.
A deficiency in its cofactor, vitamin C, is associated with scurvy.
References
- ↑ Hausmann E (Apr 1967). "Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen". Biochimica et Biophysica Acta. 133 (3): 591–3. doi:10.1016/0005-2795(67)90566-1. PMID 6033801.
- ↑ Rhoads RE, Udenfriend S (Aug 1968). "Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase". Proceedings of the National Academy of Sciences of the United States of America. 60 (4): 1473–8. doi:10.1073/pnas.60.4.1473. PMC 224943. PMID 5244754.
External links
- Lysyl+Hydroxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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