3.4.22.B77: Sulfolobus solfataricus peptidase
This is an abbreviated version!
For detailed information about Sulfolobus solfataricus peptidase, go to the full flat file.
Word Map on EC 3.4.22.B77
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3.4.22.B77
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bietti
-
dystrophy
-
retinal
-
corneoretinal
-
fundus
-
acuity
-
choroid
-
cornea
-
ophthalmic
-
electroretinography
-
coherence
-
ophthalmological
-
pigmentosa
-
intraretinal
-
full-field
-
angiography
-
slit-lamp
-
limbus
-
tiny
-
best-corrected
-
glittering
-
crystal-like
-
perimetry
-
chorioretinal
-
biomicroscopy
-
electroretinogram
- 3.4.22.B77
-
bietti
-
dystrophy
- retinal
-
corneoretinal
-
fundus
-
acuity
-
choroid
-
cornea
-
ophthalmic
-
electroretinography
-
coherence
-
ophthalmological
-
pigmentosa
-
intraretinal
-
full-field
-
angiography
-
slit-lamp
-
limbus
-
tiny
-
best-corrected
-
glittering
-
crystal-like
-
perimetry
-
chorioretinal
-
biomicroscopy
-
electroretinogram
Reaction
Hydrolysis of proteins. Preferentially cleaves -Glu-/- bonds. The enzyme is capable of cleaving Tyr-/- and Phe-/- bonds (chymotrypsin-like activity), Lys-/- and Arg-/- bonds (trypsin-like activity). Asp-/- and Asn-/- bonds are cleaved to a much lower extent. The protease degrades relatively large proteins (50 and 200 kDa) to yield small (below 500 Da) peptides. =
Synonyms
peptidase C61.001
ECTree
3.4.22.B77 Sulfolobus solfataricus peptidaseAdvanced search results
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results (Reaction
Reaction on EC 3.4.22.B77 - Sulfolobus solfataricus peptidase
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins. Preferentially cleaves -Glu-/- bonds. The enzyme is capable of cleaving Tyr-/- and Phe-/- bonds (chymotrypsin-like activity), Lys-/- and Arg-/- bonds (trypsin-like activity). Asp-/- and Asn-/- bonds are cleaved to a much lower extent. The protease degrades relatively large proteins (50 and 200 kDa) to yield small (below 500 Da) peptides.
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