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Literature summary extracted from

  • Kwon, A.R.; Kessler, B.M.; Overkleeft, H.S.; McKay, D.B.
    Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome (2003), J. Mol. Biol., 330, 185-195.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.25.2 HslU HslV can be activated by binding of a hexameric HslU(DELTAI)6 ring lacking the I domain. The activation is effected through a conformational change in hslV rather than through alteration of the size of the entry channel into the protease catalytic cavity. The two HslV6 rings in the protease dodecamer are activated independently rather than cooperatively Haemophilus influenzae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.25.2
-
 Haemophilus influenzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.25.2 asymmetric HslU(DELTAI)6HslV12 complex.HslV can be activated by binding of a hexameric HslU(DELTAI)6 ring lacking the I domain Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
3.4.25.2 Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.25.2 benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
-
 Haemophilus influenzae benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
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