Application | Comment | Organism |
---|---|---|
synthesis | application of MMP-2 from sea cucumber (Stichopus japonicas) to prepare bioactive collagen hydrolysate | Apostichopus japonicus |
Cloned (Comment) | Organism |
---|---|
MMP-2 gene cloning from the body wall of sea cucumber, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged MMP-2(111-461) comprising the catalytic domain in Escherichia coli strain BL21(DE3) in inclusion bodies | Apostichopus japonicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | can only partially complement Ca2+ for enzyme activity | Apostichopus japonicus | |
Ca2+ | Ca2+ is required for optimal gelatinolytic activity, binding structure, overview | Apostichopus japonicus | |
additional information | no activity with Fe2+, Co2+, Cu2+, Mn2+ or Mg2+ | Apostichopus japonicus | |
Zn2+ | dependent on, binding structure, overview, can only partially complement Ca2+ for enzyme activity | Apostichopus japonicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Collagen + H2O | Apostichopus japonicus | degradation of beta- and gamma-chains, weak activity with alpha-chains | ? | - |
? | |
Gelatin + H2O | Apostichopus japonicus | - |
? | - |
? | |
additional information | Apostichopus japonicus | rMMP-2 degrades collagen effectively and the hydrolysate reveals scavenging activities on both 2, 2'-diphenyl-1-picrylhydrazyl free radical and hydrogen peroxide | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Apostichopus japonicus | A0A2P9J4V0 | i.e. Stichopus japonicas | - |
Purification (Comment) | Organism |
---|---|
recombinant soluble, refolded His-tagged MMP-2(111-461) from Escherichia coli by nickel affinity chromatography (eluted with 50 mM Tris-HCl, pH 8.0, containing 300 mM NaCl, 4 M urea, and 200 mM imidazole) and dialysis | Apostichopus japonicus |
Renatured (Comment) | Organism |
---|---|
refolding of recombinant His-tagged MMP-2(111-461) from Escherichia coli strain BL21(DE3) dissolved with 4 M urea from inclusion bodies | Apostichopus japonicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Collagen + H2O | degradation of beta- and gamma-chains, weak activity with alpha-chains | Apostichopus japonicus | ? | - |
? | |
Gelatin + H2O | - |
Apostichopus japonicus | ? | - |
? | |
additional information | rMMP-2 degrades collagen effectively and the hydrolysate reveals scavenging activities on both 2, 2'-diphenyl-1-picrylhydrazyl free radical and hydrogen peroxide | Apostichopus japonicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 40000, recombinant MMP-2(111-461), SDS-PAGE, x * 70890, sequence calculation | Apostichopus japonicus |
More | the deduced amino acid sequence of MMP-2 contains a signal peptide, a propeptide domain, a catalytic domain with three repeats of fibronectin-type II region and a C-terminal hemopexin-like domain. Three-dimensional and secondary enzyme structure analysis | Apostichopus japonicus |
Synonyms | Comment | Organism |
---|---|---|
matrix metalloproteinase-2 | - |
Apostichopus japonicus |
MMP-2 | - |
Apostichopus japonicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
recombinant enzyme | Apostichopus japonicus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
56.8 | - |
denaturation temperature of recombinant MMP-2 | Apostichopus japonicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
recombinant enzyme | Apostichopus japonicus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 10 | activity range, recombinant enzyme, no activity below or above | Apostichopus japonicus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Apostichopus japonicus | sequence calculation | - |
5.05 |