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3.4.24.35: gelatinase B

This is an abbreviated version!
For detailed information about gelatinase B, go to the full flat file.

Word Map on EC 3.4.24.35

Reaction

Cleavage of gelatin types I and V and collagen types IV and V =

Synonyms

92 kDa gelatinase, 92 kDa type IV collagenase, 92 kDa type IV collagenase proMMP-9, 92-kDa Gelatinase, 92-kDa gelatinase B, 92-kDa Type IV collagenase, 95 kDa type IV collagenase/gelatinase, Collagenase IV, Collagenase type IV, gelatinase, gelatinase B, Gelatinase MMP 9, gelatinolytic enzyme, GELB, Macrophage gelatinase, matrix metallopeptidase 9, matrix metallopeptidase 9 gelatinase B, matrix metalloprotease-9, Matrix metalloproteinase 9, matrix metalloproteinase-9, metrix metalloproteinase-9, MMP 9, MMP-9, MMP9, neutrophil collagenase, pro-matrix metalloproteinase-9, progelatinase, Type IV collagen metalloproteinase, Type IV collagenase, Type IV collagenase/gelatinase, Type V collagenase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.35 gelatinase B

Molecular Weight

Molecular Weight on EC 3.4.24.35 - gelatinase B

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
SDS-PAGE
103000
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
104000
-
gel filtration
105000
-
the molecular mass of recombinant MMP-9 is approximately 105000 Da, SDS-PAGE
130000
135000
-
neutrophil gelatinase-associated lipocalin-MMP-9 complex, SDS-PAGE
150000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 150000 Da band represents a complex of MMP-9 with itself, other matrix metallproteinases, or other molecules such as TIMPs or inflammatory molecules
200000
-
the molecular weight of proMMP-9 is about 200000 Da, SDS-PAGE
20947
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
210000
dimeric form, SDS-PAGE
220000
-
native PAGE
225000
228300
enzyme multimer/trimer, PAGE, structure analysis by AFM
230000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
65000
65000 - 82000
major circulating MMP-9 enzyme forms: 92 kDa proMMP-9, and active 82 kDa and 65 kDa enzyme forms
66000
-
active form of MMP-9, SDS-PAGE
67000
-
active form of MMP-9, SDS-PAGE
70795
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
72000
-
active form of MMP-9, SDS-PAGE
78000
-
active form of MMP-9, SDS-PAGE
80000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
82000
84000
85000
-
85000 Da polypeptide in both cellular and secreted parasite extracts, activated form of MMP-9, SDS-PAGE
86000
87000
-
active form of MMP-9
88000
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
94000
95000
-
proMMP-9, SDS-PAGE
96000
-
proMMP-9, SDS-PAGE
97000