3.4.21.B3: duodenase
This is an abbreviated version!
For detailed information about duodenase, go to the full flat file.
Word Map on EC 3.4.21.B3
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3.4.21.B3
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duodenal
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mucosa
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cathepsins
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mast
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soybean
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brunner
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granzymes
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chymases
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par1
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enteropeptidase
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antichymotrypsin
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zymogen
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janus-faced
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chymotrypsinogen
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beta-hexosaminidase
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degranulation
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biotechnology
-
analysis
- 3.4.21.B3
- duodenal
- mucosa
- cathepsins
-
mast
- soybean
-
brunner
-
granzymes
- chymases
- par1
- enteropeptidase
- antichymotrypsin
- zymogen
-
janus-faced
- chymotrypsinogen
- beta-hexosaminidase
-
degranulation
- biotechnology
- analysis
Reaction
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro =
Synonyms
ChlD, chymotrypsin-like duodenase, DSD, dual-specificity duodenase, duodenase, duodenase I, duodenase serine protease, duodenase-like protein, granzyme-like protein III
ECTree
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Reaction
Reaction on EC 3.4.21.B3 - duodenase
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proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
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proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
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proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine, catalytic triad H57, D107, and S195
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
belongs to the group of Janus-faced proteinases with dual specificity
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
serine protease which has a dual specificity, i.e. both trypsin-like and chymotrypsin-like activities