Information on EC 3.4.24.B3 - matrix metalloproteinase-11

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The expected taxonomic range for this enzyme is: Tetrapoda

EC NUMBER
COMMENTARY hide
3.4.24.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
matrix metalloproteinase-11
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
145267-01-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Balb/c mice
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-N3-(2,4-dinitrophenyl)-L-2,3-diamino propionylamide + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-N3-(2,4-dinitrophenyl)-L-2,3-diamino propionylamide
show the reaction diagram
-
-
-
?
a1-PI + H2O
?
show the reaction diagram
-
-
-
-
?
aggrecan + H2O
?
show the reaction diagram
-
28 kDa N-terminal domain, cartilage proteoglycan encapsulated in polyacrylamide beads
-
?
alpha1-antitrypsin inhibitor + H2O
?
show the reaction diagram
-
-
-
?
alpha1-protease inhibitor + H2O
?
show the reaction diagram
carboxymethylated transferrin + H2O
?
show the reaction diagram
-
28 kDa N-terminal domain
-
?
casein + H2O
?
show the reaction diagram
collagen type IV + H2O
?
show the reaction diagram
collagen VI + H2O
?
show the reaction diagram
dansyl-Ala-Ala-Ala-S-(phenylmethyl)cysteine-Trp-Ala-Arg-NH2 + H2O
dansyl-Ala-Ala-Ala + S-(phenylmethyl)cysteine-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-(2S)-2-aminoheptanoyl-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (2S)-2-aminoheptanoyl-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-(2S)-2-aminooctanoyl-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (2S)-2-aminooctanoyl-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-(5-phenyl)Nva-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (5-phenyl)Nva-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
dansyl-Pro-Leu-Ala-Met-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
dansyl-Pro-Leu-Ala-Nle-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-Phe-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Ala-S-p-methoxybenzylcysteine-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
wild-type and mutants Q215R and Q215L, mutant Q215Y shows no activity with this substrate
-
?
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
show the reaction diagram
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Ser-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Ser-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
dansyl-Pro-Leu-Phe-S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Phe + S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
28 kDa N-terminal domain
-
?
GAAGAMFLEA + H2O
GAAGA + MFLEA
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
28 kDa N-terminal domain, low activity
-
?
GGAANLVRGG + H2O
GGAAN + LVRGG
show the reaction diagram
-
-
-
?
GGPLALWARGG + H2O
GGPLA + LWARGG
show the reaction diagram
-
-
-
?
GGPLGLYAGG + H2O
GGPLG + LYAGG
show the reaction diagram
-
-
-
?
GGQPRGVWGG + H2O
GGQPRG + VWGG
show the reaction diagram
-
-
-
?
GGTDAWLSGG + H2O
GGTDA + WLSGG
show the reaction diagram
-
-
-
?
GGYAELRMGG + H2O
GGYAE + LRMGG
show the reaction diagram
-
best substrate
-
?
Human alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
preferred cleavage site: (A)/(G/A)(A)(M)(F/A)(L) (P3-P3') inability of Xenopus alpha1-proteinase inhibitor to be cleaved
-
-
?
insulin-like growth factor-binding protein-1 + H2O
2 peptides of 16 and 9 kDa MW
show the reaction diagram
-
specific for, cleavage site is the His140-Val141 bond
-
?
Laminin + H2O
?
show the reaction diagram
laminin receptor precursor + H2O
?
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
collagen VI + H2O
?
show the reaction diagram
laminin receptor precursor + H2O
?
show the reaction diagram
-
laminin receptor precursor is a likely in vivo substrate of stromelysin-3. Its cleavage may alter cell-extracellular matrix interaction, thus playing a role in mediating the effects of stromelysin-3 on cell fate and behavior observed during development and pathogenesis. Human laminin receptor precursor is cleaved by stromelysin-3 at the same two sites as in Xenopus laminin receptor precursor, yielding two N-terminal fragments of sizes identical to the corresponding Xenopus laminin receptor precursor fragments due to amino acid insertion in the C-terminus part of Xenopus laminin receptor precursor
-
-
?
protein + H2O
peptides
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
-
3 zinc atoms per enzyme molecule, metalloproteinase, the zinc binding site is catalytically active
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
cephalosporine EK2900
-
-
-
matrix metalloprotease inhibitor TIMP-2
-
matrix metalloproteinase inhibitor AG3340
-
broad spectrum inhibitor
matrix metalloproteinase inhibitor BB-94
-
-
matrix metalloproteinase inhibitor TIMP-1
-
complete inhibition, human
-
matrix metalloproteinase inhibitor TIMP-2
-
-
-
N-alpha-(2-[[(1-[[(4,6-dichloro-1H-indol-2-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(6,8-dichloro-2-oxo-2H-chromen-3-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-naphthalen-2-ylbutanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-D-tryptophanamide
-
1% residual activity at 0.002 mM
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
RXP03
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-6-phenylhexanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]tetradecanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[3-(benzyloxy)propanoyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[N-(3-chlorophenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(2-[[(1-[[N-(5-chloro-2-hydroxyphenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(cyclohexylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(decylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(naphthalen-2-ylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methylpropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-phenylethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-ethoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxyphenyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methylbutyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-chlorobenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(furan-2-ylmethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(1-methylethyl)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[3-(trifluoromethoxy)biphenyl-4-yl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[4-bromo-2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(phenylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,4-di-tert-butylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,5-dimethoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-bromophenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[2-([[1-(acetylamino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-alanyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-leucyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-([[1-[[(benzyloxy)carbonyl]amino]-2-(3-bromophenyl)ethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-benzyl-3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[2-[(hydroxy[1-[(1H-indol-2-ylcarbonyl)amino]-2-phenylethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-[(hydroxy[2-phenyl-1-[(N-phenyl-b-alanyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[2-[(hydroxy[2-phenyl-1-[(quinolin-2-ylcarbonyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-(naphthalen-2-ylmethyl)propanoyl]-L-tryptophanamide
-
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-methylpropanoyl]-L-tryptophanamide
-
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-[(benzylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
-
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-3-[(3,5-dinitrophenyl)amino]-L-alaninamide
-
-
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-alaninamide
-
20% residual activity at 0.002 mM
phenylmethylsulfonyl fluoride
-
slight inhibition
phosphinic inhibitor
-
TIMP-1
-
; tissue inhibitor of metalloproteinases
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminophenylmercuric acetate
CD47
-
extracellular matrix metalloproteinase inducer, CD147 depletion in Hca-F cells results in the significantly decreased expression of matrix metalloproteinase-11
-
thyroid hormone T3
Trypsin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.088
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2
0.0045 - 0.0064
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
0.294 - 0.705
GGAANLVRGG
0.148 - 0.207
GGYAELRMGG
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
substrate specificity with synthetic substrates
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.038
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2
0.078 - 0.65
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
0.69 - 6.08
GGAANLVRGG
0.58 - 6.08
GGYAELRMGG
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
Mus musculus
-
substrate specificity with synthetic substrates
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000006
matrix metalloproteinase inhibitor AG3340
-
pH 7.6, 37C
0.0000009
N-alpha-(2-[[(1-[[(4,6-dichloro-1H-indol-2-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000005
N-alpha-(2-[[(1-[[(6,8-dichloro-2-oxo-2H-chromen-3-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000022
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-tryptophanamide
-
-
0.000015
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-naphthalen-2-ylbutanoyl)-L-tryptophanamide
-
-
0.000009
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
-
0.000005
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000033
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-6-phenylhexanoyl)-L-tryptophanamide
-
-
0.000034
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]tetradecanoyl)-L-tryptophanamide
-
-
0.000051
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
-
0.0001
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000005
N-alpha-(2-[[(1-[[3-(benzyloxy)propanoyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000004
N-alpha-(2-[[(1-[[N-(3-chlorophenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.00001
N-alpha-(2-[[(1-[[N-(5-chloro-2-hydroxyphenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
-
0.000002
N-alpha-(3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.00026
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(cyclohexylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
0.00005
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(decylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
0.000026
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(naphthalen-2-ylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
-
0.00053
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.0003
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000165
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methylpropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.00008
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-phenylethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000275
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-ethoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.00038
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000066
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxyphenyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000165
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methylbutyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000017
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-chlorobenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000002
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.000033
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(furan-2-ylmethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
-
0.0003
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(1-methylethyl)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
0.000413
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
0.000615
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[3-(trifluoromethoxy)biphenyl-4-yl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
0.00033
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[4-bromo-2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
-
0.00001
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(phenylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
-
0.000077
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,4-di-tert-butylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
0.00043
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,5-dimethoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
0.000113
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-bromophenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
0.00027
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
0.00023
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
-
0.00002
N-alpha-[2-([[1-(acetylamino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.000008
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-alanyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.000006
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-leucyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.000005
N-alpha-[2-([[1-[[(benzyloxy)carbonyl]amino]-2-(3-bromophenyl)ethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.00035
N-alpha-[2-benzyl-3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]propanoyl]-L-tryptophanamide
-
-
0.0000015
N-alpha-[2-[(hydroxy[1-[(1H-indol-2-ylcarbonyl)amino]-2-phenylethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.000015
N-alpha-[2-[(hydroxy[2-phenyl-1-[(N-phenyl-b-alanyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.0000042
N-alpha-[2-[(hydroxy[2-phenyl-1-[(quinolin-2-ylcarbonyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
-
0.000016
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
-
0.000175
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
-
0.000074
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-(naphthalen-2-ylmethyl)propanoyl]-L-tryptophanamide
-
-
0.0027
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-methylpropanoyl]-L-tryptophanamide
-
-
0.000036
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-[(benzylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
-
0.000027
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-3-[(3,5-dinitrophenyl)amino]-L-alaninamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
recombinant processed and truncated enzyme, substrate beta-casein
21
-
purified recombinant latently active enzyme form
99
-
purifed recombinant active enzyme form
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.5 - 7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
subcutaneous and gonadal adipose tissue
Manually annotated by BRENDA team
-
increased expression of MMP11 at mRNA and protein levels in cell lines and primary tumors of gastric cancer. Overexpression of MMP11 induced proliferation and invasion in AGS cells
Manually annotated by BRENDA team
-
MMP11 protein is frequently detected in sera of common cancer patients including gastric cancer
Manually annotated by BRENDA team
-
mouse colon cancer cells
Manually annotated by BRENDA team
-
larval intestinal
Manually annotated by BRENDA team
-
ST-3+/TIMP-2- (stromelysin-3+/matrix metalloproteinase TIMP-2)-phenotype is an adverse prognosticator in esophageal cancer patients
Manually annotated by BRENDA team
-
BGC823. MMP11 may play an important role in the control of cell proliferation and tumor development in gastric cancer
Manually annotated by BRENDA team
-
expression of stromelysin-3 (matrix metalloproteinase-11) in macrophages of murine thymus following thymocyte apoptosis
Manually annotated by BRENDA team
-
upregulation of stromelysin-3 in the thymus following thymocyte apoptosis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
x * 21000, recombinant processed and truncated form, SDS-PAGE
22000
-
x * 22000, recombinant processed and truncated form, SDS-PAGE
28000
-
x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE
44000
-
x * 44000, active processed form, SDS-PAGE
55000
-
x * 55000, proenzyme form, SDS-PAGE
58000
-
x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE
120000
-
x * 120000, SDS-PAGE; x * 120000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain complexed with a phosphinic inhibitor mimicking the transition state, hanging drop method, 5 mg/ml protein in 0.05 M MES, pH 5.5, 0.5 M ammonium sulfate, 1% v/v trifluoroethanol, 4C, a few months, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
enzyme complexed with a phosphinic inhibitor, inhibitor to protein ratio is 2.2:1, in presence of detergent CHAPS, hanging drop method, 5 mg/ml protein in 0.05 M MES, pH 5.5, 0.5 M ammonium sulfate, 1% v/v trifluoroethanol, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cibacron-Blue 3GA-CL agarose column chromatography, gelatin Sepharose column chromatography, and heparin Sepharose column chromatography
-
recombinant catalytic domain and mutants from Escherichia coli
-
recombinant catalytic domain expressed in Escherichia coli with a recovery of 7%
-
recombinant enzyme from Escherichia coli and NSO mouse myeloma cells
-
recombinant from Escherichia coli, addition of CHAPS, i.e. 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate, to avoid protein aggregation, binding mechanism
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 and MDA-MB-330 cells
-
expressed in Escherichia coli TOP 10 cells
expressed in MCF-7 cells and MDA-MB-231 cells
-
expression in Escherichia coli BL21(DE3)
-
expression in MCF-7 breat adenocarcinoma cells, secretion of the enzyme
-
expression of an inactive enzyme in Escherichia coli BL21(DE3), expression of a functional enzyme in NSO mouse myeloma cell line
-
expression of catalytic domain connected to the hemopexin-like domain in Escherichia coli BL21(DE3)
-
expression of catalytic site comprising residues 98-272 and of mutants A235P and E216A in Escherichia coli
-
expression of enzyme residues Phe102-Ser276 in Escherichia coli BL21(DE3)
-
expression of truncated mutant lacking the N-terminal prodomain in Escherichia coli BL21(DE3), and the C-terminal part of the hemopexin-like domain, expression of wild-type enzyme in MFC7 cells
-
expression of truncated mutant lacking the N-terminal prodomain, the C-terminal part of the hemopexin-like domain, and mutant A235P in Escherichia coli BL21(DE3)
-
from NIH-3T3 cells, establishing of a chemically induced, MMP11-overexpressing colon cancer model, overview
-
MMP-11 expression analysis
-
MMP-11 expression in healthy and cancer tissues, overview
-
MMP11, expression analysis
-
MP-11 expression analysis
-
overexpression of the catalytic domain in Escherichia coli BL21(DE3)
-
overexpression of wild-type and mutant E220A in Escherichia coli, expression of wild-type and inactive enzyme in MCF7 carcinoma cells
the enzyme lacking the signal and propeptide is expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is upregulated 4323times in canine mammary tumor state compared to normal mammary gland tissue
-
ST3 is thyroid hormone T3-inducible in Xenopus laevis. the mRNA is strongly upregulated by stage 58 in the tadpole intestine, prior to any detectable epithelial apoptosis
-
stromelysin-3 is slightly downregulated in obese adipose tissue compared to non-obese adipose tissue
-
treatment of BCS-TC2 cells with butyrate and trichostatin A (histone deacetylase inhibitors) increases MMP11 promoter activity 1.5-2fold and protein expression 1.4-1.7fold. Sp1 is involved in MMP11 basal expression and is essential for the upregulation of transcription by histone deacetylase inhibitors. ERK1/2-mitogen-activated protein kinase, but not p38-MAPK or JNK, is involved in the upregulation of MMP11 by histone deacetylase inhibitors
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A38V
polymorphismsm rs738792, T/C, may be associated with Kawazaki disease in the Korean population
E220A
-
site-directed mutagenesis, exchange of a residue in the zinc-binding catalytic domain, inactive
P235A
-
site-directed mutagenesis, truncated mutant with this introduces point mutation shows reduced enzyme activity against laminin and collgen IV
Q215L
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
Q215R
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
Q215Y
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzyme are solubilized and refolded from inclusion bodies after expression in Escherichia coli
-
recombinant truncated enzyme is solubilized and refolded from inclusion bodies after expression in Escherichia coli
-
refolding of recombinant enzyme from inclusion bodies after overexpression in Escherichia coli
renaturation from inclusion bodies after expression in Escherichia coli
-
solubilization and refolding of recombinant catalytic enzyme domain from inclusion bodies after expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
pharmacology
-
enzyme form with the specific residue A235 is an attractive target for the development of specific inhibitors for use in prevention of cancer progression