The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. (Q27919632)

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The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro

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English	The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro.	scientific article	The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro

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scholarly article

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26 November 2016

Europe PubMed Central

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15 December 2019

The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro (English)

1 reference

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15 December 2019

1

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15 December 2019

4

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15 December 2019

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Raili Myllylä

6

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15 December 2019

Lahja Uitto

5

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15 December 2019

Jari Heikkinen

3

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15 December 2019

Hanne Luosujärvi

2

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15 December 2019

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1 November 2002

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15 December 2019

2 references

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15 December 2019

21

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15 December 2019

559-566

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15 December 2019

7

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15 December 2019

Overhydroxylation of lysyl residues is the initial step for altered collagen cross-links and fibril architecture in fibrotic skin

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Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity.

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Collagen Glycosyltransferases

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Urinary galactosyl-hydroxylysine in postmenopausal osteoporotic women: A potential marker of bone fragility

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Assay of Collagen‐Galactosyltransferase and Collagen‐Glucosyltransferase Activities and Preliminary Characterization of Enzymic Reactions with Transferases from Chick‐Embryo Cartilage

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Collagen glucosyltransferase. Partial purification and characterization of the enzyme from whole chick embryos and chick-embryo cartilage

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Identification of arginine-700 as the residue that binds the C-5 carboxyl group of 2-oxoglutarate in human lysyl hydroxylase 1.

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Cloning and characterization of a third human lysyl hydroxylase isoform

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Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity

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Collagens: molecular biology, diseases, and potentials for therapy

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Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity

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Affinity chromatography of collagen glycosyltransferases on collagen linked to agarose

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Partial purification and characterization of collagen galactosyltransferase from chick embryos

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Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse.

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Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3).

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Caenorhabditis elegans

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10.1016/S0945-053X(02)00071-9

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mapped directly with Wikidata item

2 references

26 November 2016

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15 December 2019

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