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Literature summary for 3.4.24.35 extracted from

  • Vandooren, J.; Born, B.; Solomonov, I.; Zajac, E.; Saldova, R.; Senske, M.; Ugarte-Berzal, E.; Martens, E.; Van Den Steen, P.; Van Damme, J.; Garcia-Pardo, A.; Froeyen, M.; Deryugina, E.; Quigley, J.; Moestrup, S.; Rudd, P.; Sagi, I.; Opdenakker, G.
    Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1 (2015), Biochem. J., 465, 259-270.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the wild-type and mutant zymogen in Spodoptera frugiperda Sf9 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information generation of the catalytically inactive mutant of zymogen proMMP-9, proMMP-9 MutE Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
tissue inhibitor of metalloproteinases 1 TIMP-1, the zymogen proMMP-9 trimers possess a 50fold higher affinity for TIMP-1 than the monomers, with a higher extent of TIMP-1 inhibition of angiogenesis induced by trimers compared with monomers Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ enzyme contains a Zn2+ -binding domain Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
89300
-
 x * 89300, about, SDS-PAGE, the natural zymogen proMMP-9 occurs as monomers, homomultimers and heterocomplexes. MMP-9 homomultimers are reduction-sensitive trimers, three-dimensional structure molecular modeling, overview. Homomultimerization of the enzyme involves cysteine bridge formation. The zymogen proMMP-9 monomer includes the propeptide, the fibronectin-like domain, the Zn2+ -binding domain, the catalytic domain, the flexible OG domain, and the haemopexin-like domain Homo sapiens
228300
-
 enzyme multimer/trimer, PAGE, structure analysis by AFM Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gelatin + H2O Homo sapiens
-
 ?
-
 ?
additional information Homo sapiens the enzyme cleaves many substrates ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P14780
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme is produced by most cell types as a zymogen, proMMP-9 Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant zymogen from Sf9 insect cells by gelatin affinity chromatography Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
macrophage
-
 Homo sapiens
-
neutrophil
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gelatin + H2O
-
 Homo sapiens ?
-
 ?
additional information the enzyme cleaves many substrates Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
? x * 89300, about, SDS-PAGE, the natural zymogen proMMP-9 occurs as monomers, homomultimers and heterocomplexes. MMP-9 homomultimers are reduction-sensitive trimers, three-dimensional structure molecular modeling, overview. Homomultimerization of the enzyme involves cysteine bridge formation. The zymogen proMMP-9 monomer includes the propeptide, the fibronectin-like domain, the Zn2+ -binding domain, the catalytic domain, the flexible OG domain, and the haemopexin-like domain Homo sapiens

Synonyms

Synonyms Comment Organism
gelatinase B
-
 Homo sapiens
MMP-9
-
 Homo sapiens

General Information

General Information Comment Organism
additional information the enzyme cleaves many substrates and is produced by most cell types as a zymogen, proMMP-9, in complex with the tissue inhibitor of metalloproteinases-1, TIMP-1, molecular modelling, overview Homo sapiens