LH3 TYR114ALA
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.	SiMPLOD3-262
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	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	+/-
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	Scietti et al., 2018 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	The structural and biochemical role of Tyr114 is described by Scietti et al. Tyr114 is involved in UDP uracil moiety stabilization. Recombinant expression of Tyr114Ala mutant yielded folded, but almost completely inactive PLOD3 variant in glycosyltranferase assays. Tyr114 is part of a non-canonical DxxD motif where Asp112 and Asp115 are responsible for Mn2+ coordination.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH3 molecular structure	Interacts with UDP
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD2-1050: LH2a PHE114ILE (SNP) SiMPLOD3-649: LH3 TYR114TYR (SNP)
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)