PLOD3

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3, also known as PLOD3, is a human gene.cite web | title = Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8985| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8985| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Salo AM, Wang C, Sipilä L, "et al." |title=Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. |journal=J. Cell. Physiol. |volume=207 |issue= 3 |pages= 644–53 |year= 2006 |pmid= 16447251 |doi= 10.1002/jcp.20596
*cite journal | author=Otsuki T, Ota T, Nishikawa T, "et al." |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Hillier LW, Fulton RS, Fulton LA, "et al." |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Wang C, Luosujärvi H, Heikkinen J, "et al." |title=The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. |journal=Matrix Biol. |volume=21 |issue= 7 |pages= 559–66 |year= 2003 |pmid= 12475640 |doi=
*cite journal | author=Rautavuoma K, Takaluoma K, Passoja K, "et al." |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 23084–91 |year= 2002 |pmid= 11956192 |doi= 10.1074/jbc.M112077200
*cite journal | author=Ruotsalainen H, Vanhatupa S, Tampio M, "et al." |title=Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. |journal=Matrix Biol. |volume=20 |issue= 2 |pages= 137–46 |year= 2001 |pmid= 11334715 |doi=
*cite journal | author=Heikkinen J, Risteli M, Wang C, "et al." |title=Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36158–63 |year= 2000 |pmid= 10934207 |doi= 10.1074/jbc.M006203200
*cite journal | author=Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI |title=Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). |journal=Matrix Biol. |volume=19 |issue= 1 |pages= 73–9 |year= 2000 |pmid= 10686427 |doi=
*cite journal | author=Passoja K, Rautavuoma K, Ala-Kokko L, "et al." |title=Cloning and characterization of a third human lysyl hydroxylase isoform. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10482–6 |year= 1998 |pmid= 9724729 |doi=
*cite journal | author=Valtavaara M, Szpirer C, Szpirer J, Myllylä R |title=Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 12881–6 |year= 1998 |pmid= 9582318 |doi=

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