3.4.22.59: caspase-6
This is an abbreviated version!
For detailed information about caspase-6, go to the full flat file.
Word Map on EC 3.4.22.59
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3.4.22.59
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caspases
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bcl-2
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alzheimer
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neurodegenerative
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pro-apoptotic
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huntington
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lamins
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apoptosis-related
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parp
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executioner
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caspase-dependent
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anti-apoptotic
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polyadp-ribose
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tunel
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caspase-mediated
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casps
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jurkat
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bid
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pan-caspase
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zvad-fmk
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apaf-1
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medicine
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procaspase-3
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fadd
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diagnostics
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fas-associated
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drug development
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molecular biology
- 3.4.22.59
-
caspases
- bcl-2
- alzheimer
- neurodegenerative
-
pro-apoptotic
- huntington
- lamins
-
apoptosis-related
- parp
-
executioner
-
caspase-dependent
-
anti-apoptotic
-
polyadp-ribose
-
tunel
-
caspase-mediated
-
casps
-
jurkat
- bid
-
pan-caspase
- zvad-fmk
- apaf-1
- medicine
- procaspase-3
- fadd
- diagnostics
-
fas-associated
- drug development
- molecular biology
Reaction
strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-/- =
Synonyms
apoptotic protease Mch-2, C14.005, Cas6, Casp-6, Casp.6, Casp6, caspase 6, caspase-6, caspase-6A, caspase-6B, Csp-6, Csp6, HLcaspase-6, MCH2, Pfcasp-6, VEIDase
ECTree
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Subunits
Subunits on EC 3.4.22.59 - caspase-6
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dimer
homodimer
2 * 32183.5, mass spectrometry, dimer: 63070, multi-angle light scattering, 58000, ultracentrifugation, after proteolytic maturation each subunit of the active enzyme is a two-chain molecule consisting of the p18 (19668.1 Da, residues 24-179) and p11 (12563.5 Da, residues 194-293), mass spectrometry
additional information
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x * 35000, Western blot analysis, small subunit (15000) resulting from cleavage at Asp194
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x * about 30000, caspase-6 with a 23-amino-acid deletion in the pro-domain, SDS-PAGE
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procaspase 6, SDS-PAGE, chemical cross-linking and gel filtration, nearly identical CD spectra of rCaspase 6 and D316A caspase 6, indicating that overal structures of both precursor and mature forms of caspase 6 should be almost indistinguishable
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cyclin B1 migrates anomalously on SDS-PAGE with 48 kDa predicted size versus 67 kDa experimental size
additional information
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activation by proteolytic self-cleavage, during activation, the N-terminal prodomain is removed by cleavage at a TETD site. Double cleavage in an unstructured linker region at a DVVD and a TEVD site gives rise to a large 20-kDa and a small 10-kDa subunit. The two large p20 and two small p10 subunits then assemble to form the active CASP6 complex
additional information
active canonical conformation of the apoenzyme apo-caspase-6, comparison to the apostructure of pH-inactivated caspase-6,crystal structure analysis, overview. Caspase-6 subunits p20 and p10 comprise residues 24179 and 194293, respectively