3.4.24.B4: matrix metalloproteinase-13
This is an abbreviated version!
For detailed information about matrix metalloproteinase-13, go to the full flat file.
Word Map on EC 3.4.24.B4
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3.4.24.B4
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cartilage
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chondrocytes
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osteoarthritis
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metalloproteinases
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joint
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articular
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aggrecan
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degeneration
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mmp-2
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tnf
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knee
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timp-1
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arthritis
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synovial
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interleukin-1
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proteoglycans
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degener
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cox-2
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osteoblast
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adamts-5
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ligament
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intra-articular
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collagenases
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col2a1
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thrombospondin
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pulposus
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runx2
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cruciate
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zymography
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chondrogenic
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gelatinase
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meniscus
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intervertebral
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subchondral
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disintegrin
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endochondral
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safranin
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synoviocytes
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collagenolytic
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matrix-degrading
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chondroprotective
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ossification
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temporomandibular
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mt1-mmp
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chondrogenesis
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medicine
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stromelysin-1
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diagnostics
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cartilage-specific
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condylar
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analysis
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osteophyte
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drug development
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aggrecanase
- 3.4.24.B4
- cartilage
- chondrocytes
- osteoarthritis
- metalloproteinases
- joint
-
articular
- aggrecan
- degeneration
- mmp-2
- tnf
- knee
- timp-1
- arthritis
- synovial
- interleukin-1
- proteoglycans
-
degener
- cox-2
- osteoblast
- adamts-5
- ligament
-
intra-articular
- collagenases
-
col2a1
- thrombospondin
- pulposus
- runx2
-
cruciate
-
zymography
-
chondrogenic
- gelatinase
- meniscus
-
intervertebral
-
subchondral
-
disintegrin
-
endochondral
-
safranin
- synoviocytes
-
collagenolytic
-
matrix-degrading
-
chondroprotective
-
ossification
-
temporomandibular
- mt1-mmp
-
chondrogenesis
- medicine
- stromelysin-1
- diagnostics
-
cartilage-specific
-
condylar
- analysis
- osteophyte
- drug development
- aggrecanase
Reaction
proteolytic degradation of proteins =
Synonyms
collagenase, collagenase 3, collagenase-3, M10.013, matrix metalloproteinase 13, matrix metalloproteinase-13, MMP-13, MMP13, MMP13a, More, UMRCASE
ECTree
3.4.24.B4 matrix metalloproteinase-13Advanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.B4 - matrix metalloproteinase-13
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu + Gly-Leu-Dpa-Ala-Arg-NH2
-
-
-
-
?
2,4-dinitrophenyl-GPLGMRSGL-NH2 + H2O
2,4-dinitrophenyl-GPLGM + RSGL-NH2
-
-
-
?
alpha1-Antichymotrypsin + H2O
?
-
cleavage of peptide bond Ala362-Leu363
-
?
alpha2-antichymotrypsin + H2O
?
-
degradation, cleavage site is Ala362-Leu363
-
?
alpha2-chain of type IV collagen + H2O
?
-
cleavage sites at amino acid residues 881 and 1000 in the triple-helical region
-
?
alpha4-chain of type IV collagen + H2O
?
-
cleavage site at amino acid residue 86 in the triple-helical region
-
?
collagen II + H2O
?
complete degradation by the isolated catalytic domain
-
-
?
collagen type I beta1,2 chain + H2O
collagen type I alpha1,2 chain
-
wild-type enzyme and enzyme fragment 249-451
-
?
Collagen type III + H2O
?
-
5 to 6fold less active compared to substrate collagen type II
-
?
collagen type IV chain alpha1 + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IV chain alpha2 + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type X + H2O
48 kDa fragment
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wild-type enzyme and enzyme fragment 249-451
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?
collagen type X + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
fibronectin + H2O
fragments of MW 100 kDa, 43 kDa, 35 kDa, and 29 kDa
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native and recombinant substrate, whole substrate molecule and fragments, wild-type enzyme and enzyme fragment 249-451
from intact plasma fibronectin
?
interstitial collagen type II + H2O
?
-
fibrillar collagen, best substrate, cleavage sites are Gly906-Leu907, Gly909-Gln910, and Gly912-Ile913
-
?
Transforming growth factor + H2O
?
-
cleavage site at amino acid residue 150 in the latency-associated peptide
-
?
type-II collagen + H2O
?
-
the osteoarthritic cartilage type-II collagen is preferentially cleaved by the proinflammatory cytokine-induced MMP-13
-
-
?
Y(NO2)GGPAGLYEK(Abz)G + H2O
Y(NO2)GGPAG + LYEK(Abz)G
FRET substrate, cleavage rate is 0.468 nmoles/second
-
-
?
Y(NO2)GPLGMRGLK(Abz)G + H2O
Y(NO2)GPLG + MRGLK(Abz)G
FRET substrate, cleavage rate is 0.006 nmoles/second
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
-
-
?
Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5 + H2O
?
-
colorimetric substrate
-
-
?
Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5 + H2O
?
-
colorimetric substrate
-
-
?
aggrecan + H2O
?
-
cleavage site in the interglobular domain is PEN341-FFG
-
?
Collagen type I + H2O
?
-
fibrillar, 5 to 6fold less active compared to substrate collagen type II
-
?
Collagen type I + H2O
?
-
wild-type enzyme, substrate binding is mediated by the C-terminal domain, which is essential for the triple helicase activity
-
?
Collagen type I + H2O
?
-
Interstitial fibers of collagen type I in the plaque can be degraded by MMP13 specifically. MMP13 is capable of degrading collagen type I in the upstream atherosclerotic lesions
-
-
?
collagen type IV + H2O
?
-
substrate alpha2-chain and alpha1-chain, wild-type enzyme and enzyme fragment 249-451
-
?
collagen type IV + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type IX + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IX + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type XIV + H2O
?
-
alpha3-chain, wild-type enzyme and enzyme fragment 249-451
-
?
collagen type XIV + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
fibrillin-1 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
fibrillin-2 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
Fibronectin + H2O
?
partial degradation by the isolated catalytic domain
-
-
?
Gelatin + H2O
?
complete degradation by the isolated catalytic domain
-
-
?
large tenascin C isoform + H2O
?
-
no activity with the small isoform
-
?
large tenascin C isoform + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
protein + H2O
peptides
-
substrate specificity and cleavage site determination via phage display approach
-
?
protein + H2O
peptides
enzyme is involved in human breast cancer pathology and in arthritic processes
-
?
protein + H2O
peptides
-
enzyme is involved in tumor progression, significant role in the turnover of connective tissue matrix constituents
-
?
protein + H2O
peptides
-
enzyme plays a key role in the matrix metalloproteinase activation cascade, and in tumor invasion and metastasis, and appears to be critical in bone metabolism and homeostasis
-
?
type II collagen + H2O
?
-
the hemopexin domain of the protease is critical for substrate specificity
-
-
?
additional information
?
-
-
plasmin-activated MMP-13 can functions as an angiogenic factor. Physiological role of MMP-13: associated with cartilage/bone resorption and collagen remodeling involved in the angiogenic cascade
-
-
?
additional information
?
-
-
collagen type XI is not cleaved by wild-type enzyme and truncated mutant
-
?
additional information
?
-
-
no activity with the minor cartilage collagen type XI
-
?
additional information
?
-
-
enzyme expression is limited to situations of rapid extracellular matrix remodeling, transcriptional regulatory mechansim, strict regulation of expression
-
?
additional information
?
-
-
role for enzyme in regulating dermal fibroblast survival, proliferation, and interaction in 3D collagen
-
-
?
additional information
?
-
-
MMP-13 has wide substrate specificity compared with other MMPs
-
-
?
additional information
?
-
-
MMP-13 interacts with tissue inhibitor of metalloproteinase-3, fibronectin 1, insulin-like growth factor binding protein 5, and FBJ murine osteosarcoma viral oncogene homologue
-
-
?
additional information
?
-
-
MMP-13 is basically capable of degrading all components of the extracellular matrix
-
-
?
additional information
?
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
stimulates bradykinin-induced tyrosine phosphorylation and activation of epidermal growth factor receptor
-
-
?
additional information
?
-
-
MMP-13 degrades intact collagen and participates in situations where rapid and effective remodeling of collagenous extracellular matrix is required
-
-
?
additional information
?
-
-
osteoblastic osteosarcoma cell line UMR 106-01, Ca2+-dependent binding in a two-step mechanism via the required specific 170 kDa enzyme receptor and the required 600 kDa LDL-receptor, internalization and degradation of the enzyme, modeling, the enzyme also binds to mouse fibroblastic cells
-
?
additional information
?
-
-
decrease in types I and III collagen with a concurrent increase in MMP-13 after elastase perfusion in males compared with females, overview
-
-
?
additional information
?
-
-
rat MMP13 is a better gelatinase than a collagenase. Injection of catalytically active recombinant MMP13 enzyme into a rat knee joint to induce cartilage damage
-
-
?
