Collagen synthesis enzyme (null)

Molecular Classification

Enzyme, Oxidoreductase (for hydroxylases), Transferase (for glycosyltransferases), Ligase (for crosslinking enzymes like lysyl oxidase)

Other Names

Prolyl 4-hydroxylase, Lysyl hydroxylase, Procollagen galactosyltransferase, Collagen prolyl 3-hydroxylase, Lysyl oxidase (LOX), Collagen-modifying enzymes

Disease Roles

Connective tissue disorders (e.g., Ehlers-Danlos syndrome)Scurvy (vitamin C deficiency affecting hydroxylation)Fibrosis

Collagen synthesis enzyme Overview

Collagen synthesis enzymes are a group of intracellular and extracellular enzymes essential for the post-translational modification and maturation of procollagen into functional collagen fibers. The most critical among them are: Prolyl 4-hydroxylases catalyze the hydroxylation of proline residues in procollagen chains—a step necessary for stabilizing the triple helix structure. This reaction requires vitamin C as a cofactor; deficiency leads to scurvy[1][2][3][4][6][7][9]. Lysyl hydroxylases modify lysine residues to hydroxylysines, which serve as sites for further glycosylation and cross-link formation[2][3][4]. Procollagen galactosyltransferases add sugar moieties to hydroxylysines[3]. After secretion from cells, lysyl oxidases catalyze oxidative deamination on specific lysine/hydroxylysine side chains—crucial for forming covalent crosslinks that stabilize mature fibrillar collagens[2]. These modifications ensure proper folding, stability, secretion, assembly into fibrils/fibers, and mechanical properties required by tissues such as skin, bone, cartilage, tendons[1]. Defects in any step can result in severe connective tissue diseases. The term "Collagen synthesis enzymes" is not a single canonical target but rather refers collectively to several distinct but related enzyme families involved at different steps. For structured data purposes each should be listed individually by their specific names. > "Several intra‐ and extracellular modifications are needed to make functional collagen molecules...the key roles [are] played by prolyl 4‐hydrox ylases...and lys yl hydrox ylases..."[4] > "Hydrox yl ase enzy mes add hydr ox y l groups t o pr o line an d ly s ine using cofactor vitamin C...Glucose an d galactose moieties ar e attached t o selected ly s ine hy dr oxy l groups..."[9] Because this entry refers generically/plurally rather than specifically/singularly—as per your conventions—this is not an ideal canonical target form ("is_incorrect": true). Each individual enzyme should be considered separately with its own structured entry.

Mechanism of Action

Inhibition or modulation of enzymatic activity to alter collagen maturation or deposition

Biological Functions

Post-translational modification of collagen

Hydroxylation of proline and lysine residues

Glycosylation of hydroxylysine residues

Crosslinking of collagen fibers

Disease Associations

Connective tissue disorders (e.g., Ehlers-Danlos syndrome)

Scurvy (vitamin C deficiency affecting hydroxylation)

Fibrosis

Osteogenesis imperfecta

Safety Considerations

Inhibiting these enzymes can impair wound healing and connective tissue integrity; risk of bleeding, poor skin/tendon strength.

Interacting Drugs

None are widely approved as direct drugs targeting these enzymes; some experimental inhibitors exist for fibrosis research.

Associated Biomarkers

Biomarker
Hydroxyproline levels in tissue/urine as a marker for collagen turnover