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

BRENDA support

Literature summary extracted from

  • Thuku, R.N.; Weber, B.W.; Varsani, A.; Sewell, B.T.
    Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form (2007), FEBS J., 274, 2099-2108.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.5.1 expressed in Escherichia coli strain BL21 (DE3) pLysS cells Rhodococcus rhodochrous

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.5.1 36500
-
 2 * 36500, inactive enzyme, reducing SDS-PAGE Rhodococcus rhodochrous
3.5.5.1 40000
-
 12 * 40000, active enzyme form, gel filtration Rhodococcus rhodochrous
3.5.5.1 480000
-
 gel filtration Rhodococcus rhodochrous

Organism

EC Number Organism UniProt Comment Textmining
3.5.5.1 Rhodococcus rhodochrous
-
-
-
3.5.5.1 Rhodococcus rhodochrous J1
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.5.1 proteolytic modification the recombinant enzyme undergoes posttranslational cleavage at approximately residue 327, resulting in the formation of active, helical homo-oligomers Rhodococcus rhodochrous

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.5.1 Q-Sepharose column chromatography and Sephacryl S-400 gel filtration Rhodococcus rhodochrous

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.5.1 benzonitrile + 2 H2O
-
 Rhodococcus rhodochrous benzoic acid + NH3
-
 ?
3.5.5.1 benzonitrile + 2 H2O
-
 Rhodococcus rhodochrous J1 benzoic acid + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.5.1 dimer 2 * 36500, inactive enzyme, reducing SDS-PAGE Rhodococcus rhodochrous
3.5.5.1 homododecamer 12 * 40000, active enzyme form, gel filtration Rhodococcus rhodochrous