SiMPLOD v. 0.6.2 alpha

LH3 PHE143LEU

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.
SiMPLOD3-264

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
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
WangÂ et al., 2002 - DOI - PubMed

Notes from publications
  A curated excerpt with information about the mutation from the publications found above
Wang et al. adopted site-directed mutagenesis approach to identify key residue in PLOD activity. The Phe143Leu mutation reduced glycosyltranferase activity.

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 PHE143LEU
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.	SiMPLOD3-264
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	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	WangÂ et al., 2002 - DOI - PubMed
Notes from publications A curated excerpt with information about the mutation from the publications found above	Wang et al. adopted site-directed mutagenesis approach to identify key residue in PLOD activity. The Phe143Leu mutation reduced glycosyltranferase activity.
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):