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Literature summary extracted from

  • Kaplan, O.; Bezouska, K.; Plihal, O.; Ettrich, R.; Kulik, N.; Vanek, O.; Kavan, D.; Benada, O.; Malandra, A.; Sveda, O.; Vesela, A.B.; Rinagelova, A.; Slamova, K.; Cantarella, M.; Felsberg, J.; Duskova, J.; Dohnalek, J.; Kotik, M.; Kren, V.; Martinkova, L.
    Heterologous expression, purification and characterization of nitrilase from Aspergillus niger K10 (2011), BMC Biotechnol., 11, 2.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.5.1 DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strain BL21-Gold(DE3)/pOK101/pTf16, no cleavage of the C-terminal peptide of the enzyme in the recombinant bacteria Aspergillus niger

General Stability

EC Number General Stability Organism
3.5.5.1 the purified native and recombinant enzyme are stabilized by glycine at 1% w/v, sucrose at 10% w/v, D-glucose at 10% w/v, trehalose at 10% w/v, D-sorbitol at 10% w/v, xylitol at 10% w/v, D-myo-inositol at 10%, D-glycerol at 10% w/v, and bovine serum albumin at 0.1-1.0% w/v, in different extents, overview Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.5.1 38500
-
 x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling Aspergillus niger
3.5.5.1 42700
-
 x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.5.5.1 Aspergillus niger A9QXE0
-
-
3.5.5.1 Aspergillus niger K10 A9QXE0
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.5.1 proteolytic modification the mature enzyme is reduced in size by about 4 kDa compared to the unprocessed enzyme, cleavage of the C-terminal peptide Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.5.1 recombinant enzyme 2fold from Escherichia coli strain BL21-Gold(DE3)/pOK101/pTf16, further purification of the refolded recombinant enzyme after 1 month storage by gel filtration Aspergillus niger

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.5.5.1 recombinant enzyme is fully denatured in 6 M guanidine-HCl and 2 M Tris-carboxyethylphosphine and refolded in vitro Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.5.1 2-cyanopyridine + 2 H2O
-
 Aspergillus niger pyridine 2-carboxylic acid + NH3
-
 ?
3.5.5.1 2-cyanopyridine + 2 H2O
-
 Aspergillus niger K10 pyridine 2-carboxylic acid + NH3
-
 ?
3.5.5.1 3-chlorobenzonitrile + 2 H2O
-
 Aspergillus niger 3-chlorobenzoic acid + NH3
-
 ?
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Aspergillus niger nicotinic acid + NH3
-
 ?
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Aspergillus niger K10 nicotinic acid + NH3
-
 ?
3.5.5.1 4-chlorobenzonitrile + 2 H2O
-
 Aspergillus niger 4-chlorobenzoic acid + NH3
-
 ?
3.5.5.1 4-cyanopyridine + 2 H2O
-
 Aspergillus niger pyridine 4-carboxylic acid + NH3
-
 ?
3.5.5.1 4-cyanopyridine + 2 H2O
-
 Aspergillus niger K10 pyridine 4-carboxylic acid + NH3
-
 ?
3.5.5.1 additional information substrate specificity and chemoselectivity of native and recombinant enzymes, no activity of both with 2-chlorobenzonitrile, 2-phenylpropionitrile, overview Aspergillus niger ?
-
 ?
3.5.5.1 additional information substrate specificity and chemoselectivity of native and recombinant enzymes, no activity of both with 2-chlorobenzonitrile, 2-phenylpropionitrile, overview Aspergillus niger K10 ?
-
 ?
3.5.5.1 phenylacetonitrile + 2 H2O low activity with the native enzyme, poor activity with the recombinant enzyme Aspergillus niger phenylacetic acid + NH3
-
 ?
3.5.5.1 phenylacetonitrile + 2 H2O low activity with the native enzyme, poor activity with the recombinant enzyme Aspergillus niger K10 phenylacetic acid + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.5.1 More homology modelling and molecular dynamics, overview Aspergillus niger
3.5.5.1 multimer x * 42700, recombinant enzyme, SDS-PAGE, x * 38500, native enzyme, SDS-PAGE, the multimeric nitrilase is composed of 12-16 subunits, mass spectrometry, analytical centrifugation, and dynamic light scattering, modelling Aspergillus niger

General Information

EC Number General Information Comment Organism
3.5.5.1 additional information native and recombinant Escherichia coli-expressed enzymes differ in substrate specificity, acid/amide ratio, reaction optima and stability Aspergillus niger