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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

Posttranslational Modification

Posttranslational Modification on EC 3.4.21.32 - brachyurin

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
the enzyme contains an N-myristoylation site
phosphoprotein
the enzyme contains potential phosphorylation sites, e.g. a casein kinase II phosphorylation site and a kinase C phosphorylation site
additional information