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Literature summary for 3.4.24.22 extracted from

  • Batra, J.; Robinson, J.; Soares, A.; Fields, A.; Radisky, D.; Radisky, E.
    Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: Binding studies and crystal structure (2012), J. Biol. Chem., 287, 15935-15946.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information purified proMMP-10-catalytic domain is activated overnight in the presence of the organomercurial compound 4-aminophenyl mercuric acetate Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified isolated catalytic enzyme domain in complex with inhibitor TIMP1, 1:1.2 (mol/mol) mixture of enzyme protein and fully deglycosylated TIMP-N30A mutant is concentrated to achieve a final protein concentration of 4-5 mg/ml. Crystals are grown by hanging drop vapor diffusion method at room temperature in 0.1 M sodium dihydrogen phosphate, pH 6.5, 12% w/v PEG 8000, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
tissue inhibitor of metalloproteinases 1 TIMP-1, the protein is expressed in HEK 293E cells, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-1, EC 3.4.24.17 Homo sapiens
tissue inhibitor of metalloproteinases 2 TIMP-2, the protein is expressed in HEK 293E cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular a secreted metalloproteinase Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P01033
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
Homo sapiens
-
lung cancer cell
-
Homo sapiens
-
skeletal muscle
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Pro-Leu-Gly-(2-mercapto-4-methyl-pentanoyl)-Leu-Gly-OC2H5 + H2O
-
Homo sapiens ?
-
?
additional information the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9 Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Matrix metalloproteinase-10
-
Homo sapiens
MMP-10
-
Homo sapiens
stromelysin-2
-
Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics using the isolated enzyme's catalytic domain, overview Homo sapiens
0.0000011
-
tissue inhibitor of metalloproteinases 1 catalytic enzyme domain, pH 7.0, 37°C Homo sapiens
0.0000058
-
tissue inhibitor of metalloproteinases 2 catalytic enzyme domain, pH 7.0, 37°C Homo sapiens

General Information

General Information Comment Organism
evolution despite their similar substrate specificities, the stromelysins show differential patterns of transcriptional regulation and tissue distribution that hint at distinct physiological functions in processes such as skeletal development, wound healing, and vascular remodeling Homo sapiens
additional information the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion, and Glu218 is positioned to function as a general acid/base in the hydrolysis reaction Homo sapiens
physiological function the enzyme functions in skeletal development, wound healing, and vascular remodeling. It is also implicated in lung tumorigenesis and tumor progression. Regulation of enzyme MMP-10 by tissue inhibitors of metalloproteinases Homo sapiens