In this article, we provide a review on the enzymes responsible for the proline and lysine modifications, that is collagen prolyl 4-hydroxylases, 3-hydroxylases and lysyl hydroxylases, and discuss their biological functions and involvement in diseases.

Hydroxylation of lysine residues is the first modification catalyzed by lysyl hydroxylases, and is critical for the following glycosylation and in determining the fate of covalent cross-linking. This chapter presents an overview of lysine hydroxylation and cross-linking of collagen, and the analytical methods we have developed.

A recent study on endochondral ossification has shown that hypoxia, and consequently, the activation of hypoxia-inducible transcription factor HIF-1, causes metabolic changes that regulate proline and lysine hydroxylation on collagen.

Hydroxylation of proline and lysine amino acids by hydroxylase enzyme as a posttranslational modification of proteins. Proline hydroxylation-mediated collagen modification has been studied broadly because of its crucial role in the structural physiology of the cell.

2019年6月30日 · Hydroxylation of lysine residues is the first modification catalyzed by lysyl hydroxylases, and is critical for the following glycosylation and in determining the fate of covalent cross-linking. This chapter presents an overview of lysine hydroxylation and cross-linking of collagen, and the analytical methods we have developed.

Hydroxylation of specific lysine residues is one of such unique modifications found in collagen, and the pattern/extent of this modification influences fibrillogenesis, cross-linking, and matrix mineralization.

Such modifications include hydroxylation of proline (Pro) and lysine (Lys) residues, glycosylation of specific hydroxylysine (Hyl) residues, oxidative deamination of the e-amino groups of Lys/Hyl in the telopeptide domains of the molecule, and subsequent intra/intermolecular crosslinking (2) (Fig. …

2020年9月23日 · In this article, we provide a review on the enzymes responsible for the proline and lysine modifications, that is collagen prolyl 4-hydroxylases, 3-hydroxylases and lysyl hydroxylases, and discuss their biological functions and involvement in diseases. Collagens are the most abundant proteins in the extracellular matrix (ECM).

1984年7月16日 · Hydroxylation of lysine (A) and proline (B) residues in protocollagen substrate with crude enzyme preparations con- taining different ratios of lysyl hydroxylase to prolyl 4-hydrox- ylase activity. The enzyme prepared from HT-1080 cells (O), from chick-embryo sternum (O), from chick embryo tendon (I) and from chick-embryo kidney ([3).

1984年7月16日 · The data suggest that prolyl 4-hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate: oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) and lysyl hydroxylase (peptidyllysine, 2-oxoglutarate; oxygen 5-oxidoreductase, EC 1.14.11.4) are competing for the protocollagen substrate, this competition resulting in an inhibition of the lysyl hydroxylase...