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Literature summary for 3.5.5.1 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
Search for more literature for 3.5.5.1

Cloned(Commentary)

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous
-
-
-
Rhodococcus rhodochrous J1
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Substrates and Products (Substrate)

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

Subunits

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