Lysyl oxidase

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Lysyl oxidase
Properties of human protein
Mass / length primary structure 249 amino acids
Cofactor Cu ++
Precursor Preprolysyl oxidase (417 amino acids)
Identifier
Gene name LOX
External IDs
Enzyme classification
EC, category 1.4.3.13 oxidoreductase
Response type Oxidative deamination
Substrate Peptidyl-lysine + O 2 + H 2 O
Products Peptidyl allysine + H 2 O 2 + NH 3 + H +
Occurrence
Parent taxon Vertebrates
Orthologue
human House mouse
Entrez 4015 16948
Ensemble ENSG00000113083 ENSMUSG00000024529
UniProt P28300 P28301
Refseq (mRNA) NM_001178102 NM_001286181
Refseq (protein) NP_001171573 NP_001273110
Gene locus Chr 5: 122.06 - 122.08 Mb Chr 18: 52.52 - 52.53 Mb
PubMed search 4015 16948

Cross-linking of tropocollagen

Lysyl oxidase , also known as protein lysine 6 oxidase , is an enzyme that occurs primarily in the extracellular space of the connective tissue of vertebrates . It catalyzes the oxidative deamination of lysine residues and thereby enables cross-links in collagen and elastin , whereby these proteins are mechanically stabilized. When people can copper deficiency and mutations in LOX - gene reduce the enzyme activity and these to Cutis Laxa lead.

description

Lysyl oxidase plays an important role in the cross-linking of collagen and elastin in the extracellular space. It catalyzes the synthesis of carbonyl groups on lysine and hydroxylysine residues in collagens and lysine residues in elastin. The formation of Schiff bases and aldol condensations result in cross-links. The lysyl oxidase thus creates the chemical prerequisites for the formation of collagen fibrils and elastic fibers and contributes significantly to the enzymatic stability and longevity of the fiber networks.

Lysyl oxidase belongs to the group of quinone-containing, copper-based amine oxidases and the reaction it induces depends on the cofactor lysyl-tyrosyl-quinone (LTQ). Lysyl oxidase is from the LOX - gene encodes people get from people on five chromosomal locus q23.3-q31.2 is. The gene product (pre-pro-lysyl oxidase) has an intracellular molar mass of 47 k Da immediately after translation . After glycosylation , it increases to 50 kDa. After secretion into the extracellular space, the pre-pro-lysyl oxidase is split into two fragments extracellularly by the bone morphogenetic protein 1 : the 32 kDa lysyl oxidase and an 18 kDa propeptide.

Individual evidence

  1. Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC007176. Retrieved September 20, 2011 .
  2. UniProt P28300
  3. HGNC: LOX , accessed on 21 July 2011th
  4. ^ N. Pischon: Importance of the extracellular collagen modifications for osteoblast differentiation and the formation of bone tissue. (PDF file; 311 kB) Habilitation thesis, Charité - Universitätsmedizin Berlin, 2010, p. 5f.

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