3.4.24.B12: ADAMTS5 endopeptidase
This is an abbreviated version!
For detailed information about ADAMTS5 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.B12
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3.4.24.B12
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cartilage
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osteoarthritis
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chondrocytes
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articular
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metalloproteinase
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collagen
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joint
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disintegrin
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degeneration
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adamts-4
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tnf
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proteoglycans
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knee
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intervertebral
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degener
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synovial
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cox-2
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mmp-1
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col2a1
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pulposus
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meniscus
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interleukin-1
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intra-articular
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versican
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disintegrin-like
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timp-3
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temporomandibular
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subchondral
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safranin
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cruciate
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matrix-degrading
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neoepitope
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chondroprotective
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chondrogenic
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brevican
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medicine
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mankin
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surgically-induced
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oa-like
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collagen-ii
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meniscectomy
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anti-catabolic
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cartilage-degrading
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interglobular
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dmm-induced
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condylar
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oa-related
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oa-associated
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osteophyte
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motifs-4
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osteoarthritis-like
- 3.4.24.B12
- cartilage
- osteoarthritis
- chondrocytes
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articular
- metalloproteinase
- collagen
- joint
-
disintegrin
- degeneration
- adamts-4
- tnf
- proteoglycans
- knee
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intervertebral
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degener
- synovial
- cox-2
- mmp-1
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col2a1
- pulposus
- meniscus
- interleukin-1
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intra-articular
- versican
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disintegrin-like
- timp-3
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temporomandibular
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subchondral
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safranin
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cruciate
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matrix-degrading
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neoepitope
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chondroprotective
-
chondrogenic
- brevican
- medicine
-
mankin
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surgically-induced
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oa-like
-
collagen-ii
-
meniscectomy
-
anti-catabolic
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cartilage-degrading
-
interglobular
-
dmm-induced
-
condylar
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oa-related
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oa-associated
- osteophyte
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motifs-4
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osteoarthritis-like
Reaction
proteolytic degradation of proteins =
Synonyms
a disintegrin and metalloprotease with thrombospondin motifs 5, a disintegrin and metalloproteinase with thrombospondin motifs 5, a disintegrin and metalloproteinase with thrombospondin motifs-5, a disintegrin and metalloproteinase with thrombospondin type 1 motifs, member 5, a disintegrin and metalloproteinase with thrombospondin type 1 motifs-5, a disintegrin and metalloproteinase with thrombospondin-1 motifs 5, a disintegrin-like and metalloproteinase with thrombospondin-1 motifs 5, ADAM-TS 5, ADAM-TS11, ADAM-TS5, adamalysin with thrombospondin type 1 motifs-5, ADAMTS-11, ADAMTS-5, ADAMTS-5(p45), ADAMTS-5(p60), ADAMTS-5(p85), ADAMTS-5-2, ADAMTS11, ADAMTS5, ADMP-2, Agg-2, aggrecanase 2, aggrecanase-, aggrecanase-2, implantin, M12.225
ECTree
3.4.24.B12 ADAMTS5 endopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.B12 - ADAMTS5 endopeptidase
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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
aggrecan + H2O
7 aggregan fragment
several cleavage sites are determined
product determination, overview
?
C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(Mca)-Gly-Glu-Leu-Glu-Gly-Arg-Gly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2 + H2O
?
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-
-
-
?
FAM-AELQGRPISIAK-TAMRA + H2O
?
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activity measured using a quenched fluorescent substrate
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-
?
K(6FAM)-DVQEFRGVTAVIRC(Qsy9)-KGK + H2O
K-(6FAM)-DVQE + FRGVTAVIRC(Qsy9)-KGK
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-
-
-
?
K-[6FAM]-DVQEFRGVTAVIRC-[Qsy9]-KGK + H2O
K-[6FAM]-DVQE + FRGVTAVIRC-[Qsy9]-KGK
-
-
-
?
Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2 + H2O
?
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-
-
-
?
Lys(carboxyfluorescein)-Asp-Val-Gln-Glu-Phe-Arg-Gly-Val-Thr-Ala-Val-Ile-Arg-Lys(tetramethylrhodamine)-Lys-Gly-Lys-NH2 + H2O
?
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-
-
-
?
matrilin-2 + H2O
?
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substrate contains two putative cleavage sites. The first site is located between residues D851 and L852 in the middle of the domain and the second at the boundary with the coiled-coil domain at the C-terminus. Deletion of the entire unique domain eliminates the proteolysis of matrilin-2. The first cleavage site is present in all matrilin-2 oligomers, the second cleavage site becomes apparent only in the matrilin-2 hetero-oligomers with matrilin-1 or matrilin-3
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?
o-aminobenzoyl-Thr-Glu-Ser-Glu-Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2 + H2O
o-aminobenzoyl-Thr-Glu-Ser-Glu + Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2
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recombinant ADAMTS-5 cleaves this substrate more readily than ADAMTS-4 in vitro
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-
?
VQTVTWPDMELPLPRNITEGEARGSVILTVKPIFEVSPSPLKG + H2O
?
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43mer peptide substrate
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-
?
aggrecan + H2O
2 aggrecan fragment
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cleavage site is Glu373-Ala374, reaction is relevant to cartilage degeneration in inflammatory joint diseases
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?
aggrecan + H2O
?
substrate from cartilage, N-terminal cleavage sites between glutamate and small uncharged aliphatic amino acids in nonglycosylated regions of the aggregan core protein: the interglobular domain E373-A, and within the chondroitinsulfate 2 attachment region E1666-G, E1771-A, and E1871-L
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?
aggrecan + H2O
?
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-
-
-
?
aggrecan + H2O
?
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cleavage site is Glu373-Ala374, other cleavage sites are Glu1545-Gly1546, Glu1819-Ala1820, and Glu1919-Leu1920
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?
aggrecan + H2O
?
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substrate from cartilage, extensive digestion, N-terminal cleavage sites between glutamate and small uncharged aliphatic amino acids in nonglycosylated regions of the aggregan core protein: the interglobular domain E373-A, and between chondroitin sulfate attachment sites 1 and 2 E1480-G
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?
aggrecan + H2O
?
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ADAMTS-5 is able to cleave aggrecan core protein about 1,000 times more effectively than ADAMTS-4
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?
aggrecan + H2O
?
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2 microg, 90 min, reaction stopped by addition of 21 mM EDTA
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?
aggrecan + H2O
?
ADAMTS-4 and ADAMTS-5 are the proteases responsible for the endogenous aggrecanase activity observed in IL-1beta stimulated bovine cartilage
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?
aggrecan + H2O
?
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aggrecan cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 5 (ADAMTS-5) is crucial for the breakdown of cartilage matrix during osteoarthritis, a degenerative joint disease that leads to the progressive destruction of articular structures
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?
aggrecan + H2O
?
cleavage at the Glu373-Ala374 site of aggrecan is measured
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?
aggrecan + H2O
?
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recombinant bovine aggrecan mutated at amino acids N-terminal or C-terminal to the interglobular domain cleavage site. Identification of multiple conserved amino acids within regions N- and C-terminal to the site of scission that may influence enzyme-substrate recognition, and may interact with exosites on ADAMTS-5. The S377Q mutant is extremely resistant to cleavage at Glu373-Ala374 by ADAMTS-5. Cleavage of S377T with ADAMTS-5 is also significantly inhibited compared to wild-type. The other P4'-mutant digests are similar to wild-type. Gln or Thr at the P4' position are inhibitory to ADAMTS-5 cleavage
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-
?
aggrecan + H2O
?
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ADAMTS5 is the most active aggrecanase compared to ADAMTS4 and is responsible for the generation of an oncostatin M-specific degradation pattern in the CS-2 region. ADAMTS5 has the ability to cleave at the oncostatin M-specific site adjacent to the aggrecan G3 region (Glu373-Ala374 bond). Truncation of the C-terminal TS domain or Sp domain does not affect the ability of the enzyme to cleave at this site
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?
aggrecan-interglobular domain + H2O
?
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an aggrecan peptide with the N-terminal sequence ARGSVIL is released and quantified
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?
aggrecan-interglobular domain + H2O
?
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cleavage site Glu373-Ala374 in aggrecaninterglobular domain
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-
?
proteins + H2O
peptides
strict specificity for cleavage between glutamic acid and uncharged aliphatic amino acids in the core proteins of large aggregating proteoglycans
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?
versican + H2O
?
expression of Adamts5 during neuromuscular development and in smooth muscle cells coincides with the broadly distributed proteoglycan versican, an ADAMTS5 substrate
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?
versican + H2O
?
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cleaves versican at Glu441-Ala442 within the glycosaminoglycan beta region of versican V1
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-
?
additional information
?
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interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzyme
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?
additional information
?
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interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzyme
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?
additional information
?
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interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzymew
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?
additional information
?
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recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-IGD-flag
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-
?
additional information
?
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recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-IGD-flag
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-
?
additional information
?
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ADAMTS-5 shows proteolytic activity by second TS domain and little by catalytic domain alone and exhibits 1000fold greater strength of proteolytic activities as compared to ADAMTS-4
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?
