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Literature summary for 3.4.24.24 extracted from

  • Ren, X.; Lamb, G.D.; Murphy, R.M.
    Distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers (2019), Am. J. Physiol. Cell Physiol., 317, C613-C625 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.24

Cloned(Commentary)

Cloned (Comment) Organism
gene MMP2, sequence comparisons, enzyme expression analysis Homo sapiens
gene MMP2, sequence comparisons, enzyme expression analysis Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
-
extracellular
-
 Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Rattus norvegicus
Ca2+ essential for gelatinase activity, no gelatinase activity at 1 mM Ca2+ Homo sapiens
Zn2+ zinc metalloprotease Homo sapiens
Zn2+ zinc metalloprotease Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gelatin + H2O Homo sapiens
-
 ?
-
 ?
Gelatin + H2O Rattus norvegicus
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P08253
-
-
Rattus norvegicus P33436
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification activation of pro-MMP2 to MMP-2 Rattus norvegicus
proteolytic modification p-aminophenylmercuric acetate (APMA) promotes activation of pro-MMP2 and its autocatalysis to active MMP2 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
cardiac muscle
-
 Rattus norvegicus
-
commercial preparation recombinant pro-enzyme and recombinant mature, activated enzyme Homo sapiens
-
additional information in rat soleus muscle and other tissues, pro- and active MMP2 show gelatinase activity, as well as a higher band that has been reported previously to represent a rodent-specific glycosylated MMP2 Rattus norvegicus
-
skeletal muscle distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview Homo sapiens
-
skeletal muscle distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview. On average, about 57% of the MMP2, along with most of the GAPDH, in the skinned fibers is freely diffusible in the cytosol, about 6% of the MMP2 dissociates with the subsequent 10-min Triton X-100 treatment, and about 37% of the MMP2 remains in the skinned fiber Rattus norvegicus
-
soleus
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gelatin + H2O
-
 Homo sapiens ?
-
 ?
Gelatin + H2O
-
 Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
gelatinase A
-
 Homo sapiens
gelatinase A
-
 Rattus norvegicus
Matrix metalloproteinase 2
-
 Homo sapiens
Matrix metalloproteinase 2
-
 Rattus norvegicus
matrix metalloproteinase-2
-
 Homo sapiens
matrix metalloproteinase-2
-
 Rattus norvegicus
MMP2
-
 Homo sapiens
MMP2
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens
7.5
-
 assay at Rattus norvegicus

General Information

General Information Comment Organism
physiological function the enzyme exhibits gelatinolytic activity which is enhanced by p-aminophenylmercuric acetate (APMA). The APMA treated enzyme probably also produces proteolytic products of myosin and other muscle proteins Homo sapiens