Reaction Details |
| Report a problem with these data |
Target | 72 kDa type IV collagenase |
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Ligand | BDBM11329 |
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Substrate/Competitor | BDBM11446 |
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Meas. Tech. | Carbonic Anhydrase Enzyme Inhibition Assay |
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Ki | 3.9±n/a nM |
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Citation | Scozzafava, A; Supuran, CT Carbonic anhydrase and matrix metalloproteinase inhibitors: sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes. J Med Chem43:3677-87 (2000) [PubMed] Article |
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More Info.: | Get all data from this article, Solution Info, Assay Method |
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72 kDa type IV collagenase |
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Name: | 72 kDa type IV collagenase |
Synonyms: | 72 kDa gelatinase | 72 kDa type IV collagenase precursor | CLG4A | Gelatinase A | Gelatinase A (MMP-2) | MMP2 | MMP2_HUMAN | Matrix metalloproteinase-2 | Matrix metalloproteinase-2 (MMP 2) | Matrix metalloproteinase-2 (MMP2) | Matrix metalloproteinases 2 (MMP-2) | TBE-1 |
Type: | Enzyme |
Mol. Mass.: | 73870.36 |
Organism: | Homo sapiens (Human) |
Description: | P08253 |
Residue: | 660 |
Sequence: | MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGC
PKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWD
KNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGD
GYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFN
GKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGT
SYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKY
ESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGAL
MAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQ
IRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEY
WIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDP
GFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
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BDBM11329 |
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BDBM11446 |
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Name | BDBM11329 |
Synonyms: | 2-[benzyl(1,1,2,2,3,3,4,4,4-nonafluorobutane)sulfonamido]-N-hydroxyacetamide | Hydroxamate 10 |
Type | Small organic molecule |
Emp. Form. | C13H11F9N2O4S |
Mol. Mass. | 462.288 |
SMILES | ONC(=O)CN(Cc1ccccc1)S(=O)(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)F |
Structure |
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