3.4.24.7: interstitial collagenase
This is an abbreviated version!
For detailed information about interstitial collagenase, go to the full flat file.
Word Map on EC 3.4.24.7
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3.4.24.7
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metalloproteinases
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mmp-2
-
metastasis
-
gelatinase
-
timp-1
-
zymography
-
endothelial
-
gelatin
-
angiogenesis
-
cartilage
-
fibrosis
-
basement
-
type-1
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stromelysins
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invasiveness
-
arthritis
-
dermal
-
plasminogen
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gelatinolytic
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prommp-2
-
proteinases
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integrins
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matrigel
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synovial
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pericellular
-
fibrosarcoma
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mt-mmp
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fibrillar
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procollagen
-
chondrocytes
-
matrix-degrading
-
collagenase-3
-
progelatinase
-
proenzyme
-
invadopodia
-
laminin-5
-
analysis
-
membrane-tethered
-
pharmacology
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drug development
-
triple-helical
-
diagnostics
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photoaging
-
medicine
-
batimastat
-
procollagenase
-
podosomes
-
furin
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hemopexin
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collagen-rich
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reck
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cortactin
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pro-matrix
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synthesis
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matrilysin
-
emmprin
- 3.4.24.7
- metalloproteinases
- mmp-2
- metastasis
- gelatinase
- timp-1
-
zymography
- endothelial
- gelatin
- angiogenesis
- cartilage
- fibrosis
-
basement
- type-1
- stromelysins
-
invasiveness
- arthritis
- dermal
- plasminogen
-
gelatinolytic
- prommp-2
- proteinases
- integrins
- matrigel
- synovial
-
pericellular
- fibrosarcoma
-
mt-mmp
-
fibrillar
- procollagen
- chondrocytes
-
matrix-degrading
- collagenase-3
- progelatinase
- proenzyme
-
invadopodia
- laminin-5
- analysis
-
membrane-tethered
- pharmacology
- drug development
-
triple-helical
- diagnostics
-
photoaging
- medicine
- batimastat
- procollagenase
-
podosomes
- furin
- hemopexin
-
collagen-rich
- reck
- cortactin
-
pro-matrix
- synthesis
- matrilysin
-
emmprin
Reaction
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-/-Ile in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue =
Synonyms
azocollase, collagen peptidase, collagen protease, collagenase, collagenase 1, collagenase A, collagenase MMP-1, collagenase-1, collagenolytic matrix metalloproteinase, EC 3.4.99.5, ect-MMP-14, Fibroblast collagenase, HSFC, kollaza, macrophage matrix metalloproteinase, matrix metalloproteinase 1, matrix metalloproteinase-1, matrix metalloproteinase-18, matrix-metalloproteinase-1, membrane-type 1-MMP, metallocollagenase, metalloproteinase-1, MMP-1, MMP-12, MMP-14, MMP-1A, mmp1, MT1-MMP, Myocardial collagenase, nucleolysin, soycollagestin, TC1, tumor collagenase, vertebrate collagenase
ECTree
3.4.24.7 interstitial collagenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.7 - interstitial collagenase
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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-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(dinitrophenyl)-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Arg-Pro-Lys-Pro-Val-Glu + Nva-Trp-Arg-Lys(dinitrophenyl)-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
-
degradation of synthetic substrate is pH-independent
-
-
?
(GP4Hyp)4-GPQGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4-GPQG + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
alpha1(I)772-786 THP
-
-
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2
-
-
-
?
(GP4Hyp)4GPQ-Sar-IAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQ-Sar + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
-
-
-
?
(GP4Hyp)4GPQGIAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2 + H2O
(GP4Hyp)4GPQG + IAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2
the substrate is hydrolyzed at the Gly775-Ile776 bond by the enzyme
-
-
?
2,4-dinitrophenyl-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-methyl-2-aminobenzoyl)-NH2 + H2O
?
-
-
-
?
acetyl-Pro-Ala-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Ala-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Frog
-
-
-
?
acetyl-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
acetyl-Pro-Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
acetyl-Pro-Leu-Gly-SCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5 + H2O
acetyl-Pro-Leu-Gly + HSCH[CH2CH(CH3)2]CO-Leu-Leu-OC2H5
-
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
butyloxycarbonyl-Pro-Ala-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Ala-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
butyloxycarbonyl-Pro-Gln-Gly-Ile-Ala-Gly-ethyl ester + H2O
butyloxycarbonyl-Pro-Gln-Gly + Ile-Ala-Gly-ethyl ester
Frog
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln
-
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2 + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln-Gln-Arg-Gly-Val-Val-Gly-Leu-Hyp-NH2
-
-
-
-
?
human pregnancy zone protein + H2O
?
-
cleavage sites: Gly685-Leu686, Gly687-Val688, Gly757-Ile758, Ala684-Leu684, and Ala685-Met686
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
Mca-Pro-Leu-Gly + Leu-Dpa-Ala-Arg-NH2
-
-
-
?
Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-ethyl ester + H2O
Pro-Gln-Gly + Ile-Ala-Gly-Gln-Arg-ethyl ester
Frog
-
-
-
?
rat alpha1 macroglobulin + H2O
?
-
cleavage site: His681-Leu682, Phe691-Leu692
-
-
?
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY + H2O
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLG + IAGIG-6-aminohexanoic acid-PKGY
-
fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
Frog
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
very low activity
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
Collagen + H2O
?
-
-
two collagen fragments representing 77% and 23% respectively of the length of the collagen molecule
?
Collagen + H2O
?
-
cleavage sites: of calf skin alpha1(I) chain collagen Gly775-Ile776, of calf skin collagen alpha2(I) chain Gly775-Leu776, of human liver collagen alpha1(III)chain Gly775-Ile776
-
-
?
Collagen + H2O
?
-
type X collagen, two cleavage sites, three products with 32000 Da, 18000 Da and 9000 Da chains
-
-
?
Collagen + H2O
?
-
183RWTNNFREY191, together with the C-terminal hemopexin domain, is essential for collagenolytic activity but additional structural elements in the catalytic domain are also required. These elements probably act in a concerted manner to cleave the collagen triple helix
-
-
?
Collagen + H2O
?
natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13
-
-
?
Collagen + H2O
?
-
below 30°C the enzyme catalyzes a small number of cleavages in the native collagen molecule with no loss in tertiary structure. Fragments of 75, 67, and 62% of the molecular length from the A end are formed. At 37°C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable
-
-
?
Collagen + H2O
?
natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13. Cleavage sites identified in Col I-rich ECM under proteolytic degradation by MMP-1, overview
-
-
?
collagen I alpha-1 chain + H2O
?
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain
-
-
?
collagen I alpha-1 chain + H2O
?
-
the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
collagen I alpha-2 chain + H2O
?
-
MMP-14 ectodomain preferentially cleaves the alpha-1 chain
-
-
?
collagen I alpha-2 chain + H2O
?
-
the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2
-
-
?
Collagen type III + H2O
?
ability of MMP-1 to unwind triple-helical collagen
-
-
?
Collagen type III + H2O
?
ability of MMP-1 to unwind triple-helical collagen. After binding the triple helix, the CAT domain can reorient to properly face the cleavage site. The dual Arg electrostatic ruler motif is modeled to be exposed in the type III collagen fibril. The two Arg residues found in type III collagen are conserved in the P5' and P17' subsites of types I and II collagen
-
-
?
collagen type IV alpha2 + H2O
?
cleavage at sites L715 and T917
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
-
?
Type I collagen + H2O
?
-
production of type I collagen by periodontal ligament cells
-
-
?
type III collagen + H2O
?
-
mechanism of interaction and cleavage of human type III collagen by fibroblast MMP-1 using a panel of recombinant human type III collagens containing engineered sequences in the vicinity of the cleavage site around residue I785, e.g. mutant FG-5015 I785P. Structural features of cleavage site determination in collagen type III, overview
-
-
?
fTHP-3 + H2O
additional information
-
-
the fluorogenic triple-helical substrate mimics the behavior of the native collagen substrate and may be useful for the investigation of collagenase triple-helical activity
the Gly-Leu bond is cleaved, the triple helix denatures and the two products generated are the single-stranded N-terminal peptide C6-(Gly-Pro-Hyp)5-Gly-Pro-Lys[(7-methoxycoumarin-4-yl)acetyl]-Gly-Pro-Gln-Gly and the single-stranded C-terminal peptide Leu-Arg-Gly-Gln-Lys-(2,4-dinitrophenyl)-Gly-Val-Arg-(Gly-Pro-Hyp)5-NH2
-
?
additional information
?
-
-
relative rates of hydrolysis in decreasing order: GPQGIAGQ, PSYFLNAG, GNVGLAGA
-
-
?
additional information
?
-
-
ligation of keratinocyte alpha2beta1 integrin by type 1 collagen induces expression of matrix metalloproteinase-1. The MMP-1 activity is required for the alpha2beta1 integrin-dependent migration of primary keratinocytes across collagenous matrices. MMP-1 binds to the I domain of the alpha2 intergrin subunit
-
-
?
additional information
?
-
-
matrix metalloproteinase 1 interacts with neuronal integrins and stimulates dephosphorylation of Akt and neuronal death through a non-proteolytic mechanism. MMP-1 might contribute to the neuronal damage which occurs in association with degenerative and inflammatpry conditions characterized by elevated levels of this proteinase
-
-
?
additional information
?
-
-
MMP-1 is involved in intestinal re-epithelization in vivo and is upregulated by cytokines relevant in wound repair
-
-
?
additional information
?
-
-
enzyme regulation on expression and protein levels, overview
-
-
?
additional information
?
-
-
MMP-1 is a single effector of the Raf/MEK/ERK signaling cascade, that prevents progression of melanoma from a primary to metastatic tumor
-
-
?
additional information
?
-
-
MMP1 expression is increased in Xeroderma pigmentosum, a rare, recessively inherited genetic disease characterized by skin cancer proneness and premature aging in photoexposed area
-
-
?
additional information
?
-
-
substance P up-regulates matrix metalloproteinase-1 and down-regulates collagen in human lung fibroblast, overview
-
-
?
additional information
?
-
-
active MMP-10, EC 3.4.24.22, does not cleave collagen type 1 directly, it does activate the collagenase MMP-1
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
-
MMP-1 cleaves a specific glycine-isoleucine or glycine-leucine bond in fibrillar collagens, despite the presence of this sequence in other parts of the protein
-
-
?
additional information
?
-
MMP-1 preferentially binds the alpha2(I) chain
-
-
?
additional information
?
-
several different peptoid residues are incorporated into triple helical substrates at subsites P3, P1, P1', and P10' individually or in combination, and the effects of the peptoid residues are evaluated on the activities of full-length MMP-1 and other MMPs, collagenolytic matrix metalloproteinase activities toward peptomeric triple-helical substrates, overview. Most peptomers show little discrimination between MMPs. A peptomer containing N-methyl Gly (sarcosine) in the P1' subsite and N-isobutyl Gly (Nle) in the P10' subsite is not hydrolysed by MMP-1. Also no activity with (GP4Hyp)4-GPQG-Sar-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4G-Sar-QGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQGWAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4-GPQG-NIle-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)-GNle-4Hyp(GP4Hyp)4-NH2 and Ac-(GP4Hyp)4-GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)G-Nle-4Hyp(GP4Hyp)4-NH2, 4Hyp is hydroxyproline. The P10' subsite is important for collagenous substrate interaction with MMP-1, and this interaction occurs via the HPX domain. Molecular dynamics (MD) simulations, model of MMP-1 with the alpha1(I)772-786 THP, overview
-
-
?
additional information
?
-
-
myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
-
-
?
additional information
?
-
proteomic analysis of MMP-1 activity using LC-MS/MS analysis
-
-
?
