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Literature summary for 1.14.11.4 extracted from

  • Suokas, M.; Lampela, O.; Juffer, A.H.; Myllyla, R.; Kellokumpu, S.
    Retrieval-independent localization of lysyl hydroxylase in the endoplasmic reticulum via a peptide fold in its iron-binding domain (2003), Biochem. J., 370, 913-920.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.4

Cloned(Commentary)

Cloned (Comment) Organism
expression of 40 amino acid residues of the C-terminal end of isozyme LH1 fused to human cathepsin D and c-Myc-tagged and 2 mutant variants thereof in COS-7 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
K694G site-directed mutagenesis, point mutation is introduced in the LH1 part of the expression construct comprising 40 amino acid residues of the C-terminal end of isozyme LH1, responsible for endoplasmic reticulum localization, fused to human cathepsin D and c-Myc-tagged, the exchange of the charged residue and deletion of 8 amino acids of the last 40 residues at the enzymes' C-terminal end has no effect on retention efficiency of the reporter protein, but deletion of the next 8 amino acid residues, leaving 24 residues, increases the secretion level of enzyme from the cell Homo sapiens
R693Q site-directed mutagenesis, point mutation is introduced in the LH1 part of the expression construct comprising 40 amino acid residues of the C-terminal end of isozyme LH1, responsible for endoplasmic reticulum localization, fused to human cathepsin D and c-Myc-tagged, the exchange of the charged residue and deletion of 8 amino acis of the last 40 residues at the enzymes' C-terminal end has no effect on retention efficiency of the reporter protein, but deletion of the next 8 amino acid residues, leaving 24 residues, increases the secretion level of enzyme from the cell Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum lumen Homo sapiens 5783
-
membrane peripheral Homo sapiens 16020
-
additional information a peptide fold in the iron-binding site, within the 40 amino acid residues at the C-terminus, is responsible for KDEL-receptor-independent localization in the endoplasmic reticulum Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a peptide fold in the iron-binding site, within the 40 amino acid residues at the C-terminus, is responsible for KDEL-receptor-independent localization in the endoplasmic reticulum Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen L-lysine + 2-oxoglutarate + O2 Homo sapiens hydroxylation of lysine residues in collagenous sequences procollagen 5-hydroxy-L-lysine + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 3 isozyme LH1-3
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen L-lysine + 2-oxoglutarate + O2
-
 Homo sapiens procollagen 5-hydroxy-L-lysine + succinate + CO2
-
 ?
procollagen L-lysine + 2-oxoglutarate + O2 hydroxylation of lysine residues in collagenous sequences Homo sapiens procollagen 5-hydroxy-L-lysine + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
LH
-
 Homo sapiens
lysyl hydroxylase
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 Homo sapiens