LH1 ARG718ALA
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.	SiMPLOD1-56
Isoenzyme   Follow the links to gather information about the LH1 isoenzyme	Lysyl Hydroxylase 1 (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	-
References   Publications (and associated links) describing the mutation	Passoja et al., 1998 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Passoja et al. identified the residues involved in 2-OG binding through mutagenesis approach. Arg718Ala mutation completely inactivated lysyl hydroxylase causing a 10-fold increase in the Km for 2-OG. This is consistent with our structural observations where Arg718 (extremely conserved throughout human PLOD) forms a bidentate interaction with the C-5 carboxyl group of 2-OG. Please note that in this reference aminoacid numbering differs from the one used in this database.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	Stabilizes 2-OG in LH catalytic site
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-884: LH1 ARG718HIS (SNP) SiMPLOD3-377: LH3 ARG729CYS (SNP)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (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): LH1 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)