Cloned (Comment) | Organism |
---|---|
recombinant expression in HEK-293 cells, the enzyme is secreted | Bos taurus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | - |
Bos taurus | |
EDTA | - |
Homo sapiens | |
additional information | no inhibition by AEBSF, NEM and PMSF | Bos taurus | |
additional information | no inhibition by AEBSF, NEM and PMSF | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required | Bos taurus | |
Ca2+ | required | Homo sapiens | |
Zn2+ | a zinc metalloproteinase | Bos taurus | |
Zn2+ | a zinc metalloproteinase | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
type I aminoprocollagen + H2O | Bos taurus | - |
? | - |
? | |
type I aminoprocollagen + H2O | Homo sapiens | - |
? | - |
? | |
type I procollagen + H2O | Bos taurus | - |
? | - |
? | |
type I procollagen + H2O | Homo sapiens | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | P79331 | - |
- |
Homo sapiens | O95450 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from cell-free extract by concanavalin A affinity chromatography, elution with alpha-methyl-D-mannoside, followed by heparin affinity chromatography and dialysis | Homo sapiens |
native enzyme from cell-free extract or extracellular recombinant enzyme secreted from HEK-293 cells by concanavalin A affinity chromatography, elution with alpha-methyl-D-mannoside, followed by heparin affinity chromatography and dialysis | Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | - |
Homo sapiens | - |
additional information | ADAMTS2 is immobilized in connective tissues | Bos taurus | - |
additional information | ADAMTS2 is immobilized in connective tissues | Homo sapiens | - |
skin | - |
Homo sapiens | - |
skin | from calf or fetal calf | Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | ADAMTS2 displays some affinity for type XIV collagen | Bos taurus | ? | - |
? | |
additional information | ADAMTS2 displays some affinity for type XIV collagen | Homo sapiens | ? | - |
? | |
type I aminoprocollagen + H2O | - |
Bos taurus | ? | - |
? | |
type I aminoprocollagen + H2O | - |
Homo sapiens | ? | - |
? | |
type I procollagen + H2O | - |
Bos taurus | ? | - |
? | |
type I procollagen + H2O | - |
Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADAM-TS2 | - |
Bos taurus |
ADAM-TS2 | - |
Homo sapiens |
ADAMTS2 | - |
Bos taurus |
ADAMTS2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
15 | 37 | assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 9 | assay at | Bos taurus |
7 | 9 | assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | in absence of ADAMTS2 activity (Ehlers-Danlos syndrome, dermatosparactic type) accumulation of processed alpha alpha1 and alpha2 chains, pNalpha1 and pNalpha2, is observed | Homo sapiens |
physiological function | type I collagen is a heterotrimer composed of 2 alpha1 chains and one alpha2 chain (which are the products of different genes) forming a typical triple helical domain. Besides the removal of the signal peptide, the maturation of type I procollagen into mature alpha chains involves cleavages of the aminopropeptide and the carboxypropeptide by aminoprocollagen peptidases (mainly ADAMTS2) and carboxyprocollagen peptidases (BMP1 and tolloids), respectively. In vivo in physiological conditions, only the fully processed alpha alpha1 and alpha2 chains are present in significant amounts. The excision of the aminopropeptide by ADAMTS2 converts the pro-chains into pC-chains, and the pN-chains into mature alpha chains | Bos taurus |
physiological function | type I collagen is a heterotrimer composed of 2 alpha1 chains and one alpha2 chain (which are the products of different genes) forming a typical triple helical domain. Besides the removal of the signal peptide, the maturation of type I procollagen into mature alpha chains involves cleavages of the aminopropeptide and the carboxypropeptide by aminoprocollagen peptidases (mainly ADAMTS2) and carboxyprocollagen peptidases (BMP1 and tolloids), respectively. In vivo in physiological conditions, only the fully processed alpha alpha1 and alpha2 chains are present in significant amounts. The excision of the aminopropeptide by ADAMTS2 converts the pro-chains into pC-chains, and the pN-chains into mature alpha chains | Homo sapiens |