BioPAX pathway converted from "Procollagen lysyl hydroxylases convert collagen lysines to 5-hydroxylysines" in the Reactome database. 1.14.11.4 Procollagen lysyl hydroxylases convert collagen lysines to 5-hydroxylysines Procollagen lysyl hydroxylases convert collagen lysines to 5-hydroxylysines This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> Reactome DB_ID: 113534 1 endoplasmic reticulum lumen GO 0005788 dioxygen [ChEBI:15379] dioxygen Reactome http://www.reactome.org ChEBI 15379 Reactome DB_ID: 1650779 1 2-oxoglutarate(2-) [ChEBI:16810] 2-oxoglutarate(2-) 2-ketoglutarate alpha-ketoglutarate 2-oxopentanedioic acid, ion(2-) 2-oxoglutarate ChEBI 16810 Reactome DB_ID: 10406784 1 endoplasmic reticulum membrane GO 0005789 Lysyl hydroxylases:Lysyl hydroxylase procollagen substrates [endoplasmic reticulum membrane] Lysyl hydroxylases:Lysyl hydroxylase procollagen substrates Converted from EntitySet in Reactome Reactome DB_ID: 10406762 1 Lysyl hydroxylase procollagen substrates [endoplasmic reticulum lumen] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity Converted from EntitySet in Reactome Reactome DB_ID: 10406782 1 Lysyl hydroxylases [endoplasmic reticulum membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity Danio rerio NCBI Taxonomy 7955 Reactome Database ID Release 82 10406784 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10406784 Reactome R-DRE-2023011 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DRE-2023011.1 Reactome DB_ID: 159751 1 carbon dioxide [ChEBI:16526] carbon dioxide ChEBI 16526 Reactome DB_ID: 10407119 1 Lysyl hydroxylases:Lysyl hydroxylated collagen propeptides [endoplasmic reticulum lumen] Lysyl hydroxylases:Lysyl hydroxylated collagen propeptides Converted from EntitySet in Reactome Reactome DB_ID: 10407117 1 Lysyl hydroxylated collagen propeptides [endoplasmic reticulum lumen] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity Converted from EntitySet in Reactome Reactome DB_ID: 10406782 1 Reactome Database ID Release 82 10407119 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10407119 Reactome R-DRE-2022428 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DRE-2022428.1 Reactome DB_ID: 1650769 1 succinate(2-) [ChEBI:30031] succinate(2-) succinate (-)OOC-CH2-CH2-COO(-) butanedioic acid, ion(2-) butanedioate ChEBI 30031 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Converted from EntitySet in Reactome Reactome DB_ID: 10406782 GO 0008475 GO molecular function Reactome Database ID Release 82 10407120 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10407120 Reactome Database ID Release 82 10407122 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10407122 Reactome R-DRE-1981104 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-DRE-1981104.1 Lysyl hydroxylase (LH) (E.C. 1.14.11.4) is a dimeric enzyme that catalyzes the formation of (2S,5R)-5-hydroxylysyl residues (5-Hyl) in proteins (reviewed in Myllyharju & Kivirikko 2001) within a peptide linkage at the Y position of the repeating X-Y-Gly sequence motif. The extent of 5-Hyl formation is much more variable than that of hydroxyproline. It varies between collagen types, tissues and by physiological state (Miller 1984). 5-Hyl content also differs between the helical and telopeptide domains. This and the observation that purified lysyl hydroxylase failed to hydroxylate Lys in the telopeptide domains has led to speculation that there are separate enzymes responsible for Lys hydroxylation in the helical and telopeptide domains (Royce & Barnes 1985, Gerriets et al. 1993). The LH2b isoform may be the telopeptide-specific form (Pornprasertsuk et al. 2004).<br>In human type I collagen, there are 38 residues of Lys in each alpha-1 chain (36 in the helical domain, 1 each in the C- and N-telopeptide domains) and 31 in each alpha-2 chain (30 in the helical domain,1 in the N-telopeptide and none in the C-telopeptide domains) (Yamauchi & Shiiba 2002). <br><br>LH requires ferrous iron, oxygen, 2-oxoglutarate, and ascorbate. The hydroxylation reaction occurs during collagen biosynthesis in the ER as a co- and post-translational event, before triple helix formation. Three LH isoforms have been characterized in humans, encoded by the genes PLOD1-3. The isoforms appear to have preferences for certain collagen types, e.g. LH3 preferentially binds collagen types IV, VI, XI and XII (Myllyla et al. 2007). LH3 has galactosyltransferase and glucosyltransferase activities in addition to its lysyl hydroxylase activity (Heikkinen et al. 2000, Wang et al. 2002), a multifunctionality also seen in the single C. elegans orthologue (Wang et al. 2002a, b). Hydroxylysine residues can form stable intermolecular cross-links between collagen molecules in fibrils and also represent sites for glucosyl- and galactosyl- carbohydrate attachment. <br><br>In this reaction all collagen subtypes are represented as having a single hydroxylysine. 978-0444007995 ISBN 1984 Chemistry of the collagens and their distribution Piez, K Reddi, A Extracellular Matrix Biochemistry (Book) 17516569 Pubmed 2007 Expanding the lysyl hydroxylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3) Myllylä, R Wang, C Heikkinen, J Juffer, A Lampela, O Risteli, M Ruotsalainen, H Salo, A Sipilä, L J Cell Physiol 212:323-9 11896059 Pubmed 2002 Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3) Wang, C Risteli, M Heikkinen, J Hussa, AK Uitto, L Myllyla, R J Biol Chem 277:18568-73 9582318 Pubmed 1998 Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) Valtavaara, M Szpirer, C Szpirer, J Myllylä, R J Biol Chem 273:12881-6 12475640 Pubmed 2002 The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro Wang, C Luosujärvi, H Heikkinen, J Risteli, M Uitto, L Myllylä, R Matrix Biol 21:559-66 11310942 Pubmed 2001 Collagens and collagen-related diseases Myllyharju, J Kivirikko, KI Ann Med 33:7-21 8244992 Pubmed 1993 Tendon hypertrophy is associated with increased hydroxylation of nonhelical lysine residues at two specific cross-linking sites in type I collagen Gerriets, JE Curwin, SL Last, JA J Biol Chem 268:25553-60 9054364 Pubmed 1997 Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle Valtavaara, M Papponen, H Pirttilä, AM Hiltunen, K Helander, H Myllylä, R J Biol Chem 272:6831-4 1577494 Pubmed 1992 Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2 Hautala, T Byers, MG Eddy, Roger L Shows, Thomas B Kivirikko, KI Myllylä, R Genomics 13:62-9 3931636 Pubmed 1985 Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen Royce, PM Barnes, MJ Biochem J 230:475-80 15231023 Pubmed 2004 Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells Pornprasertsuk, S Duarte, WR Mochida, Y Yamauchi, M J Bone Miner Res 19:1349-55 10934207 Pubmed 2000 Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity Heikkinen, J Risteli, M Wang, C Latvala, J Rossi, M Valtavaara, M Myllylä, R J Biol Chem 275:36158-63 6809411 Pubmed 1981 Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts Turpeenniemi-Hujanen, T M Puistola, U Kivirikko, K I Coll. Relat. Res. 1:355-66 12029842 Pubmed 2002 Lysine hydroxylation and crosslinking of collagen Yamauchi, M Shiiba, M Methods Mol Biol 194:277-90 inferred by electronic annotation IEA GO IEA