Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.6 extracted from

  • Osanai, A.; Harada, S.; Sakamoto, K.; Shimizu, H.; Inaoka, D.K.; Kita, K.
    Crystallization of mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil (2009), Acta Crystallogr. Sect. F, 65, 941-944.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized in the presence of octaethyleneglycol monododecyl ether and n-dodecyl-beta-D-maltopyranoside in a 3:2 weight ratio, crystals belongs to a orthorhombic space group with unit-cell parameters a=123.75 A, b= 29.08 A and c=221.12 A, diffracted to 2.8 A resolution using synchrotron radiation Ascaris suum

Inhibitors

Inhibitors Comment Organism Structure
flutolanil fungizide Ascaris suum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Ascaris suum 5739
-

Organism

Organism UniProt Comment Textmining
Ascaris suum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mitochondria prepared from the muscle are used for purification on a DEAE Sepharose FF column Ascaris suum

Source Tissue

Source Tissue Comment Organism Textmining
muscle from adult Ascaris suum Ascaris suum
-

Synonyms

Synonyms Comment Organism
mitochondrial rhodoquinol-fumarate reductase
-
 Ascaris suum
QFR
-
 Ascaris suum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000081
-
 promising lead compound for anthelminthics Ascaris suum flutolanil