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Information on EC 3.4.24.22 - stromelysin 2

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.22 stromelysin 2
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UNIPROT: P16035 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Similar to stromelysin 1, but action on collagen types III, IV and V is weak
Synonyms
mmp-10, mmp10, stromelysin-2, matrix metalloproteinase-10, matrix metalloproteinase 10, stromelysin 2, transin 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Matrix metalloproteinase-10
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Matrix metalloproteinase 10
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Matrix metalloproteinase-10
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MMP-10
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Proteoglycanase 2
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Transformation-associated protein 34A
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Transin 2
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Transins, 2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
140610-48-6
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tissue inhibitor of metalloproteinases 2
TIMP-2, conserved mechanism of inhibition, interactions and conformation analysis, and structural changes induced by complex formation with the enzyme's catalytic domain, detailed overview
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additional information
the endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs. Identification of a group of highly conserved contacts at the heart of MMP/TIMP complexes that define the conserved mechanism of inhibition, as well as a second category of diverse adventitious contacts at the periphery of the interfaces
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
matrix metalloproteinases (MMPs) play central roles in vertebrate tissue development, remodeling, and repair. The endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TIMP2_HUMAN
220
0
24399
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified active human MMP-10 catalytic domain in complex with inhibitor protein TIMP-2, hanging drop vapor diffusion method, mixing of proteins in a 1:1.1 (mol/mol) ratio, 4.5-5.5 mg/ml protein in 20 mM Tris, pH 8.5 and 150 mM NaCl, are mixed with reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% w/v PEG 2000 monomethyl ether, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement, comparison and analysis of the crystal structure of the human MMP-10/TIMP-1 complex, PDB ID 3V96
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme MMP-10 catalytic domain from Escherichia coli strain BL21 (DE3), by anion exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme catalytic domain in Escherichia coli strain BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Batra, J.; Soares, A.; Mehner, C.; Radisky, E.
Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes
PLoS ONE
8
e75836
2013
Homo sapiens (P16035)
Manually annotated by BRENDA team