3.4.21.103: physarolisin
This is an abbreviated version!
For detailed information about physarolisin, go to the full flat file.
Word Map on EC 3.4.21.103
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3.4.21.103
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3.4.23.6
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proteinases
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r-factors
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endothiapepsin
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renin
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rhizopuspepsin
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rhizopus
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root-mean-square
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scissile
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beta-hairpins
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pepstatin
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non-hydrogen
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penicillopepsin
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serine-carboxyl
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statine-containing
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hydroxyethylene
- 3.4.21.103
-
3.4.23.6
- proteinases
-
r-factors
- endothiapepsin
- renin
- rhizopuspepsin
- rhizopus
-
root-mean-square
-
scissile
-
beta-hairpins
- pepstatin
-
non-hydrogen
- penicillopepsin
-
serine-carboxyl
-
statine-containing
-
hydroxyethylene
Reaction
Milk clotting activity. Preferential cleavage of Gly8-/-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-/-Gly and Phe24-/-Phe. No action on Ac-Phe-Tyr(I)2. =
Synonyms
EC 3.4.23.27, EC 3.4.23.6, EC 3.4.4.17, physarolisin, physarolisin I, physarolysin II, Physarum aspartic proteinase, proteinase, Dictyostelium discoideum aspartic, proteinase, Dictyostelium discoideum aspartic, E, proteinase, Physarum flavicomum aspartic, proteinase, Physarum polycephalum acid
ECTree
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Molecular Weight
Molecular Weight on EC 3.4.21.103 - physarolisin
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23000
31000
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1 * 31000 + 1 * 23000, the two chains are cross-linked by disulfide bond(s), SDS-PAGE under reducing and nonreducing conditions
23000
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1 * 31000 + 1 * 23000, the heavy and the light chain are cross-linked by disulfide bonds, SDS-PAGE
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1 * 31000 + 1 * 23000, the two chains are cross-linked by disulfide bond(s), SDS-PAGE under reducing and nonreducing conditions
31000
-
1 * 31000 + 1 * 23000, the heavy and the light chain are cross-linked by disulfide bonds, SDS-PAGE