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3.4.21.32: brachyurin

This is an abbreviated version!
For detailed information about brachyurin, go to the full flat file.

Word Map on EC 3.4.21.32

Reaction

hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin =

Synonyms

aspergillopeptidase C, azocollase, clostridiopeptidase A, clostridiopeptidase I, clostridiopeptidase II, CLSP, collagen peptidase, collagenase, collagenase A, collagenase MMP-1, collagenolytic protease, collagenolytic serine protease, crab protease I, crab protease II, Es-CLSP, kollaza, matrix metalloproteinase-1, matrix metalloproteinase-18, Matrix metalloproteinase-8, metallocollagenase, metalloproteinase-1, MMP-1, MMP-8, non-clip domain serine protease, nucleolysin, peptidase, clostridio-, A, protease PC, proteinase, Clostridium histolyticum, A, PtSP, PtSPH1, soycollagestin, Try4, uca pugilator collagenolytic proteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.32 brachyurin

Expression

Expression on EC 3.4.21.32 - brachyurin

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression, encoded by a immune-related gene, is highly responsive to Vibrio anguillarum challenge in hemocytes/the hepatopancreas, and shows a different response to the intruding pathogens, overview
the enzyme variant PtSP shows slight increase during the first 48 h compared to control groups except 8 h point after Micrococcus luteus challenge
the expression level of enzyme variant PtSPH1 is challenged by Gram-negative bacteria Vibrio alginolyticus, Gram-positive bacteria Micrococcus luteus and fungi Pichia pastoris during the first 48 h