LH3 ARG520END
SiMPLOD ID   This is the unique identifier for this mutation in the SiMPLOD database. Please use this identifier when linking information described in SiMPLOD about this mutation.	SiMPLOD3-294
Isoenzyme   Follow the links to gather information about the LH3 isoenzyme	Lysyl Hydroxylase 3 (human) - UniProt - Full Info
Mutation type   Current information about the clinical implications of the mutation	Mutation for Biochemical Studies (not necessarily related to observed polymorphisms)
Evidence at protein level   Based on available structural and biochemical information, a statement about the existence of an LH enzyme variant bearing the described mutation is provided	Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 520, and may result in misfolding and/or complete absence of the enzyme. This variant EXISTS at the protein level: published experimental data support its existence as protein product.
LH Activity   When available, biochemical data describing the lysyl hydroxylase activity of the mutant are reported	No experimental data available
GT/GGT Activity   When available, biochemical data describing the galactosyltransferase (GT) and glucosylgalactosyltransferase (GGT) activities of the mutant are reported	+
References   Publications (and associated links) describing the mutation	Wang et al., 2002 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	To determine the PLOD3 region involved in glycosyltransferase activity Wang et al. produced several C-terminal deletion constructs. Protein were produced in E. Coli and insect cells and the activity was measured. The resulting proteins had reduced, but not eliminated glycosyltransferase activity, whereas were completely lacking lysyl-hydroxylase activity.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH3 molecular structure
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic) SiMPLOD1-185: LH1 SER510SER (Likely benign) SiMPLOD1-325: LH1 delta491-550 (Pathogenic)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH3 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH3 (generated using the crystal structure of full-length human LH3 as template). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh): LH3 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)LH3 with Fe2+, 2-OG and Mn2+ (PDB 6FXM)LH3 with Fe2+, 2-OG, Mn2+ and UDP-Gal (PDB 6FXR)LH3 with Fe2+, 2-OG, Mn2+ and UDP-Glc (PDB 6FXT)