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Literature summary for 3.4.24.22 extracted from

  • Schlage, P.; Egli, F.; Nanni, P.; Wang, L.; Kizhakkedathu, J.; Apte, S.; Keller, U.
    Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome (2014), Mol. Cell. Proteomics, 13, 580-593.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information enzyme cleavage site specificity and kinetics, overview Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADAMTS-like protein 1 + H2O Mus musculus i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24 ?
-
?
ADAMTS-like protein 1 + H2O Mus musculus BALB/c i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24 ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus O55123
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-
Mus musculus BALB/c O55123
-
-

Source Tissue

Source Tissue Comment Organism Textmining
3T3 cell
-
Mus musculus
-
fibroblast
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADAMTS-like protein 1 + H2O i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24 Mus musculus ?
-
?
ADAMTS-like protein 1 + H2O recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP Mus musculus ?
-
?
ADAMTS-like protein 1 + H2O i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24 Mus musculus BALB/c ?
-
?
ADAMTS-like protein 1 + H2O recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP Mus musculus BALB/c ?
-
?
collagen alpha-1(l) + H2O cleavage site is GPPG993-/-994LAGP Mus musculus ?
-
?
collagen alpha-1(l) + H2O cleavage site is GPPG993-/-994LAGP Mus musculus BALB/c ?
-
?
collagen alpha-2(I) + H2O cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP Mus musculus ?
-
?
collagen alpha-2(I) + H2O cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP Mus musculus BALB/c ?
-
?
collagen alpha-2(v) + H2O cleavage site is GPHG487-/-488IQGP Mus musculus ?
-
?
lysyl oxidase + H2O cleavage site is QVFS050-/-051LLSL Mus musculus ?
-
?
lysyl oxidase + H2O cleavage site is QVFS050-/-051LLSL Mus musculus BALB/c ?
-
?
platelet-derived growth factor receptor alpha + H2O cleavage into two fragments of about 40 and 80 kDa, cleavage site is VPAS416.417ILDL in the extracellular domain Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
Matrix metalloproteinase 10
-
Mus musculus
MMP10
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mus musculus

General Information

General Information Comment Organism
metabolism fibroblast secretome cleavage analysis, analysis of the MMP10 substrate degradome, overview Mus musculus
additional information enzyme cleavage site specificity, overview Mus musculus
physiological function the enzyme performs ectodomain shedding of platelet-derived growth factor receptor alpha as well as sequential processing of type I collagen Mus musculus