SiMPLOD v. 0.6.2 alpha

L230 LEU873ASP

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.
SiMPLOD4-285

Isoenzyme
  Follow the links to gather information about the L230 isoenzyme
Lysyl Hydroxylase L230 (mimivirus) - 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
No experimental data available

References
  Publications (and associated links) describing the mutation
Guo et al., 2018 - DOI - PubMed

Notes from publications
  A curated excerpt with information about the mutation from the publications found above
Guo et al. performed site-directed mutagenesis on L230, a viral homolog of PLOD3 to determine key residues in activity and dimerization. The Leu873Asp mutation (Leu715 in PLOD3) cause loss of dimerization. The enzymatic activity of this mutant was lost on collagen, but was comparable to wild-type on a synthetic collagen peptide. This suggests that dimerization is essential for binding and activity on lengthy collagen chains. Scietti et al. demonstrated that the same mutation in PLOD3 (see Leu715Asp) does not disrupt PLOD3 dimer.

Structural Observations
  An evaluation of the possible effects/implications of the mutations on the L230 molecular structure
Involved in the LH-LH dimerization interface

Last Update
  An evaluation of the possible effects/implications of the mutations on the L230 molecular structure
2021-06-23 08:38:51

The three-dimensional visualization is currently based on the dimeric structure of of the C-terminal LH domain of mimivirus L230 in complex with Fe²⁺ (from PDB id 6AX7).

You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh):

L230 LEU873ASP
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.	SiMPLOD4-285
Isoenzyme Follow the links to gather information about the L230 isoenzyme	Lysyl Hydroxylase L230 (mimivirus) - 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	No experimental data available
References Publications (and associated links) describing the mutation	Guo et al., 2018 - DOI - PubMed
Notes from publications A curated excerpt with information about the mutation from the publications found above	Guo et al. performed site-directed mutagenesis on L230, a viral homolog of PLOD3 to determine key residues in activity and dimerization. The Leu873Asp mutation (Leu715 in PLOD3) cause loss of dimerization. The enzymatic activity of this mutant was lost on collagen, but was comparable to wild-type on a synthetic collagen peptide. This suggests that dimerization is essential for binding and activity on lengthy collagen chains. Scietti et al. demonstrated that the same mutation in PLOD3 (see Leu715Asp) does not disrupt PLOD3 dimer.
Structural Observations An evaluation of the possible effects/implications of the mutations on the L230 molecular structure	Involved in the LH-LH dimerization interface
Last Update An evaluation of the possible effects/implications of the mutations on the L230 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the dimeric structure of of the C-terminal LH domain of mimivirus L230 in complex with Fe²⁺ (from PDB id 6AX7). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh):