3.4.24.B10: ADAM12 endopeptidase
This is an abbreviated version!
For detailed information about ADAM12 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.B10
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3.4.24.B10
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adams
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pregnancy
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trimester
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integrins
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metalloproteinases
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myoblasts
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papp-a
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pregnancy-associated
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preeclampsia
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first-trimester
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ectodomain
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thrombospondin
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protein-a
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hb-egf
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egf-like
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metalloprotease-disintegrins
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gestation-specific
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nuchal
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disintegrin-like
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timp-3
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adamts-7
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invadopodia
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medicine
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metalloproteinase-12
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beta-hcg
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prodomain
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second-trimester
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igfbp-5
- 3.4.24.B10
-
adams
- pregnancy
-
trimester
- integrins
- metalloproteinases
- myoblasts
- papp-a
-
pregnancy-associated
- preeclampsia
-
first-trimester
- ectodomain
- thrombospondin
- protein-a
- hb-egf
-
egf-like
-
metalloprotease-disintegrins
-
gestation-specific
-
nuchal
-
disintegrin-like
- timp-3
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adamts-7
-
invadopodia
- medicine
-
metalloproteinase-12
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beta-hcg
- prodomain
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second-trimester
- igfbp-5
Reaction
proteolysis of proteins =
Synonyms
a disintegrin and metalloprotease 12, a disintegrin and metalloprotease with thrombospondin motifs 12, a disintegrin and metalloprotease-12, a disintegrin and metalloproteinase 12, a disintegrin and metalloproteinase domain 12, a disintegrin and metalloproteinase domain-containing protein 12, a disintegrin and metalloproteinase12, ADAM 12, ADAM 12-S, ADAM-12, ADAM-12m, ADAM-PCD, ADAM12, ADAM12-L, ADAM12-PC, ADAM12-S, ADAM12/meltrin alpha, ADAM12L, ADAM12S, ADAMTS-12, ADMA12L, basigin sheddase, disintegrin and metalloprotease 12, full-length ADAM 12-S, M12.212, meltrin alpha, meltrin-alpha, metalloprotease-disintegrin ADAM 12, metalloprotease-disintegrin ADAM12
ECTree
3.4.24.B10 ADAM12 endopeptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.24.B10 - ADAM12 endopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C179A
C179H
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain, still active in complex formation with alpha2-macroglobulin
C179H/E351Q
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain results in a no longer latent but inactive zymogen
C179S
E351Q
G48R
naturally occuring mutation, statistically significant association between this polymorphism and patellofemoral osteoarthritis in male patients
L792F
the mutant with wild type activity is not associated with breast cancer
D301H
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the mutation ihibits the proteolytic processing and activation of ADAM12
G479E
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the mutation ihibits the proteolytic processing and activation of ADAM12
L73P
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mutant with properties similar to wild-type concerning the cell cycle of C2C12 cells
L792F
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the mutation ihibits the proteolytic processing and activation of ADAM12
additional information
C179A
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain results in a no longer latent but inactive zymogen
C179A
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain, still active in complex formation with alpha2-macroglobulin
C179S
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain results in a no longer latent but inactive zymogen
C179S
site-directed mutagenesis, exchange of the cysteine-switch residue of the prodomain the glutamic acid residue and of the zinc binding domain involved in catalytic activity, inactive to form complexes with alpha2-macroglobulin, results in a no longer latent but inactive zymogen
C179S
site-directed mutagenesis, mutant behaves identical to the wild-type concerning metal ions, therfore the cysteine-switch and activation by copper are 2 different components of enzyme activation
E351Q
site-directed mutagenesis, exchange of the glutamic acid residue of the zinc binding domain involved in catalytic activity, inactive to form complexes with alpha2-macroglobulin
additional information
elimination of the cysteine-switch by a point mutation in the propeptide has no effect on copper activation, whereas mutation of an unpaired cysteine residue in the catalytic domain resulted in a mutant form of ADAM 12-S that is insensitiv to copper
additional information
KR207NG mutation prevents cleavage of the prodomain by furin, construction of enzyme mutants where the prodomain or the metalloprotease domain or both are eliminated or exchanged for an Ig kappa-chain leader sequence, secretion to the medium, inactive mutant
additional information
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KR207NG mutation prevents cleavage of the prodomain by furin, construction of enzyme mutants where the prodomain or the metalloprotease domain or both are eliminated or exchanged for an Ig kappa-chain leader sequence, secretion to the medium, inactive mutant
additional information
construction of deletion mutants comprising the cytoplasmic tail with or without the alpha-actinin-2-binding site
