PLOD3 explained
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.[1] [2] [3]
The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.
Further reading
- Salo AM, Wang C, Sipilä L, etal . Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. . J. Cell. Physiol. . 207 . 3 . 644–653 . 2006 . 16447251 . 10.1002/jcp.20596 . 19594208 .
- Otsuki T, Ota T, Nishikawa T, etal . Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. . DNA Res. . 12 . 2 . 117–126 . 2007 . 16303743 . 10.1093/dnares/12.2.117 . free .
- Rual JF, Venkatesan K, Hao T, etal . Towards a proteome-scale map of the human protein-protein interaction network. . Nature . 437 . 7062 . 1173–1178 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 .
- Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–2127 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
- Hillier LW, Fulton RS, Fulton LA, etal . The DNA sequence of human chromosome 7. . Nature . 424 . 6945 . 157–164 . 2003 . 12853948 . 10.1038/nature01782 . 2003Natur.424..157H . free .
- Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–16903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
- Wang C, Luosujärvi H, Heikkinen J, etal . The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. . Matrix Biol. . 21 . 7 . 559–566 . 2003 . 12475640 . 10.1016/S0945-053X(02)00071-9 .
- Rautavuoma K, Takaluoma K, Passoja K, etal . Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1–3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity. . J. Biol. Chem. . 277 . 25 . 23084–23091 . 2002 . 11956192 . 10.1074/jbc.M112077200 . free .
- Ruotsalainen H, Vanhatupa S, Tampio M, etal . Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. . Matrix Biol. . 20 . 2 . 137–146 . 2001 . 11334715 . 10.1016/S0945-053X(01)00130-5 .
- Heikkinen J, Risteli M, Wang C, etal . Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. . J. Biol. Chem. . 275 . 46 . 36158–36163 . 2000 . 10934207 . 10.1074/jbc.M006203200 . free .
- Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI . Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). . Matrix Biol. . 19 . 1 . 73–79 . 2000 . 10686427 . 10.1016/S0945-053X(99)00058-X .
Notes and References
- Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI . Cloning and characterization of a third human lysyl hydroxylase isoform . Proc Natl Acad Sci U S A . 95 . 18 . 10482–10486 . Sep 1998 . 9724729 . 27920 . 10.1073/pnas.95.18.10482 . free . 1998PNAS...9510482P .
- Valtavaara M, Szpirer C, Szpirer J, Myllyla R . Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) . J Biol Chem . 273 . 21 . 12881–12886 . Jun 1998 . 9582318 . 10.1074/jbc.273.21.12881 . free .
- Web site: Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3.