Literature summary for 3.4.25.2 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.

Search for more literature for 3.4.25.2

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

Cloned (Comment)	Organism
-	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)