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3.4.22.32: Stem bromelain

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

Word Map on EC 3.4.22.32

Reaction

broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates =

Synonyms

acidic bromelain stem proteinase, ACMD2_17643, BRM, Bromelain, Bromelain, stem, EC 3.4.22.4, EC 3.4.4.24, Pineapple stem bromelain, SBA, Sbm, stem bromelain

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.32 Stem bromelain

pH Stability

pH Stability on EC 3.4.22.32 - Stem bromelain

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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.8 - 2
-
stem bromelain at pH 2.0 is maximally unfolded and characterized by significant loss of secondary structure (about 80%) and almost complete loss of tertiary contacts, at pH 0.8 a molten globule state is observed with secondary structure content similar to that of native protein but no tertiary structure
680545
2
-
almost complete loss of native tertiary contacts, acid unfolded state
664339
3 - 9
-
4°C, 24 h, stable
30285
3.2 - 7
-
stem bromelain solubilized at pH 7.0 and at pH 3.2 retains, after 16 h at 256°C, 10 and 40% of the initial activity, respectively
731526
4 - 10
-
5°C, 24 h, stable
30273
5
-
50°C, 60 min, stable
30285
5.5 - 10
-
stem bromelain is fully resistant against urea around neutral pH (5.5 to 10.0) and unfolds only below pH 5.0
707537
5.6 - 9
-
stable
30297
7 - 10
-
from pH 7.0 to 10.0, the protein's secondary structure remains the same, although a slight loss of tertiary structure is observed. Above pH 10.0, there is a significant and irreversible loss of secondary and tertiary structure. At pH 10.0, SBM shows a significant increase in 8-anilino-1-naphthalene-sulfonate binding relative to the native state. No significant loss of activity is observed up to pH 10.0, beyond which there is an irreversible loss of activity
707283