SiMPLOD v. 0.6.2 alpha

LH1 ASN197GLN

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.
SiMPLOD1-58

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
Pirskanen et al., 1996 - DOI - PubMed

Notes from publications
  A curated excerpt with information about the mutation from the publications found above
Pirskanen et al. performed site directed mutagenesis to identify PLOD1 glycosylation sites. Mutations involving Asn163 and Asn686 did not affect protein mobility in SDS-PAGE whereas mutation of Asn197 and Asn538 shifted mobility toward lower molecular weights. This suggests that only two of the four potential N-glycosylation sites (Asn197 and Asn538) are effectively glycosylated.

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 ASN197GLN
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.	SiMPLOD1-58
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	Pirskanen et al., 1996 - DOI - PubMed
Notes from publications A curated excerpt with information about the mutation from the publications found above	Pirskanen et al. performed site directed mutagenesis to identify PLOD1 glycosylation sites. Mutations involving Asn163 and Asn686 did not affect protein mobility in SDS-PAGE whereas mutation of Asn197 and Asn538 shifted mobility toward lower molecular weights. This suggests that only two of the four potential N-glycosylation sites (Asn197 and Asn538) are effectively glycosylated.
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):