3.4.22.31: Ananain
This is an abbreviated version!
For detailed information about Ananain, go to the full flat file.
Reaction
hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-/-NHMec, but broader specificity than fruit bromelain =
Synonyms
bromelain protease F9
ECTree
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Subunits
Subunits on EC 3.4.22.31 - Ananain
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additional information
modeling of three-dimensional structure, enzyme lacks the extensive network of acidic residues in and around the active site
additional information
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modeling of three-dimensional structure, enzyme lacks the extensive network of acidic residues in and around the active site
additional information
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ananain exhibits a typical papain-like domain organization: an alpha-helix abundant L-domain comprised of residues 10-111 and 208-215, and a beta-sheet rich R-domain consisting of residues 1-9 and 112-207. In between the two domains there are two pocket-like structures, marked as pocket 1 and pocket 2. Pocket 1 is formed by the side chains of Gln19, Gly23, Trp26, Gly64, Trp180 and most importantly, the active site residues Cys25 and His157, the latter two residues essentially forming a catalytic diad. In contrast to pocket 1, which is geometrically flat and open, pocket 2 is deep and narrow, formed by the side chains of a number of hydrophobic residues, including Trp26, Trp66, Ile67, Ala132, Leu155 and Ala158