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Literature summary for 3.4.25.2 extracted from

  • Koodathingal, P.; Jaffe, N.E.; Kraut, D.A.; Prakash, S.; Fishbain, S.; Herman, C.; Matouschek, A.
    ATP-dependent proteases differ substantially in their ability to unfold globular proteins. (2009), J. Biol. Chem., 284, 18674-18684.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Cloned(Commentary)

Cloned (Comment) Organism
HslU and HslV were coexpressed in BL21 (DE3) pLysS cells Haemophilus influenzae
HslU and HslV were coexpressed in BL21 (DE3) pLysS cells Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barnase-DHFR fusion proteins + H2O
-
 Haemophilus influenzae ?
-
 ?
barnase-DHFR fusion proteins + H2O
-
 Escherichia coli ?
-
 ?
additional information degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction Haemophilus influenzae ?
-
 ?
additional information degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ClpYQ
-
 Haemophilus influenzae
ClpYQ
-
 Escherichia coli
HslUV
-
 Haemophilus influenzae
HslUV
-
 Escherichia coli