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Literature summary for 2.4.1.66 extracted from

  • Salo, A.M.; Cox, H.; Farndon, P.; Moss, C.; Grindulis, H.; Risteli, M.; Robins, S.P.; Myllylae, R.
    A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene (2008), Am. J. Hum. Genet., 83, 495-503.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information A668G, higher apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and about 80% reduced glucosyltransferase activity, about 50% decreased lysyl hydroxylase activity, EC 1.14.11.4 Homo sapiens
additional information delT2071, lower apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and about 50% reduced glucosyltransferase activity, complete loss of lysyl hydroxylase activity, EC 1.14.11.4 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
value about, Western blot Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lymphoblastoid cell line
-
Homo sapiens
-
serum
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
25 DMP/microg soluble protein, control group, activitiy in lymphoblastoid cells Homo sapiens
additional information
-
25 DPM/microl serum, patient with mutation of the lysyl hydroxylase 3 gene Homo sapiens
additional information
-
5 DPM/microg soluble protein, patient with mutation of the lysyl hydroxylase 3 gene, activitiy in lymphoblastoid cells Homo sapiens
additional information
-
800 DPM/microl serum, control group Homo sapiens

General Information

General Information Comment Organism
malfunction disorders of LH3 with a unique phenotype causing severe morbidity as a result of feauters that overlap with collagen disorders Homo sapiens
physiological function forms part of the many posttranslational modifications required during collagen biosynthesis Homo sapiens