Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.11.4 extracted from

  • Ruotsalainen, H.; Risteli, M.; Wang, C.; Wang, Y.; Karppinen, M.; Bergmann, U.; Kvist, A.P.; Pospiech, H.; Herzig, K.H.; Myllylae, R.
    The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin (2012), PLoS ONE, 7, e50045.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.4

Protein Variants

Protein Variants Comment Organism
D669A site-directed mutagenesis, inactive mutant Mus musculus
additional information generation of an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Mus musculus C57BL/6
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Mus musculus
-

Synonyms

Synonyms Comment Organism
LH3
-
 Mus musculus
lysyl hydroxylase 3
-
 Mus musculus

General Information

General Information Comment Organism
malfunction lack of LH3 prevents the formation of hydroxylysine linked Glc-Gal structures in collagen. Secretion of type IV collagen is blocked in embryos that lack LH3 catalyzed Glc-Gal-Hyl residues, and this disrupts formation of the basement membranes that support tissues e.g. blood vessels. Changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion, phenotype, overview. Recombinant adiponectin produced in LH3-/- knockout fibroblasts cells does not form middle molecular weight and high molecular weight oligomers Mus musculus
physiological function regulation of the posttranslational lysine modifications in the collagenous domain is the key event in determining the function of adiponectin, changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion Mus musculus