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

BRENDA support

Literature summary for 3.5.1.4 extracted from

  • Nel, A.J.; Tuffin, I.M.; Sewell, B.T.; Cowan, D.A.
    Unique aliphatic amidase from a psychrotrophic and haloalkaliphilic Nesterenkonia isolate (2011), Appl. Environ. Microbiol., 77, 3696-3702.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.4

Cloned(Commentary)

Cloned (Comment) Organism
gene nitN, DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli Nesterenkonia sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, hanging drop vapour diffusion, from 0.1 M sodium acetate trihydrate, and 2 M ammonium sulfate, pH 4.6, single wavelengh X-ray diffraction structure determination and analysis at 1.7 A resolution Nesterenkonia sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27950
-
 2 * 27950, about, sequence calculation Nesterenkonia sp.

Organism

Organism UniProt Comment Textmining
Nesterenkonia sp. C6K3Z5 isolated from mineral soil collected from the Miers Valley, McMurdo region, eastern Antarctica
-
Nesterenkonia sp. AN1 C6K3Z5 isolated from mineral soil collected from the Miers Valley, McMurdo region, eastern Antarctica
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Nesterenkonia sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme NitN has an active site and a fold characteristic of the nitrilase superfamily, but shows only amidase activity, no nitrilase activity Nesterenkonia sp. ?
-
 ?
additional information the enzyme NitN has an active site and a fold characteristic of the nitrilase superfamily, but shows only amidase activity, no nitrilase activity Nesterenkonia sp. AN1 ?
-
 ?
propanamide + H2O
-
 Nesterenkonia sp. propanoic acid + NH3
-
 ?
propanamide + H2O
-
 Nesterenkonia sp. AN1 propanoic acid + NH3
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 27950, about, sequence calculation Nesterenkonia sp.
More one active site per monomer, the active-site cysteine lies in a solvent-accessible pocket, structure analysis, overview Nesterenkonia sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Nesterenkonia sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5
-
 Nesterenkonia sp.