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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.5.5 - Arylacetonitrilase and Organism(s) Aspergillus niger and UniProt Accession A2R6M7

for references in articles please use BRENDA:EC3.5.5.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.5 In nitriles
                3.5.5.5 Arylacetonitrilase
IUBMB Comments
Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aspergillus niger
UNIPROT: A2R6M7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Aspergillus niger
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
arylacetonitrilase, gpnor51, nitmp, nitan, nitrilase ppl19, blr3397, enantioselective arylacetonitrilase, arylacetonitrile-hydrolyzing nitrilase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arylacetonitrilase
-
Nitrilase, arylaceto-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of nitriles
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Arylacetonitrile aminohydrolase
Requires thiol compounds. Also hydrolyses other 4-substituted phenylacetonitriles, thien-2-ylacetonitrile, tolylacetonitriles, and, more slowly, benzyl cyanide.
CAS REGISTRY NUMBER
COMMENTARY hide
132053-06-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-2-phenylpropionitrile + 2 H2O
2-phenylpropionic acid + NH3
show the reaction diagram
the enzyme produces (R)-2-phenylpropionic acid with an e.e.-value of 90% at 28% conversion
-
-
?
(R,S)-mandelonitrile + 3 H2O
mandelic acid + mandelamide + NH3
show the reaction diagram
the enzyme produces almost no mandelamide at pH 5 (Fig. 1a), while the R-acid is formed with a high enantiomeric excess
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
show the reaction diagram
i.e. (R,S)-mandelonitrile
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
show the reaction diagram
phenylpropionitrile + 2 H2O
phenylpropionate + NH3
show the reaction diagram
-
-
-
?
(S)-mandelonitrile + 2 H2O
(R)-mandelic acid + NH3
show the reaction diagram
-
the enzyme produces up to more than 70 g/l of (R)-mandelic acid (enantiomeric excess 94.5-95.6%) in batch or fed-batch mode. Its volumetric productivities are the highest in batch mode (571 g/l*d) and its catalyst productivities in fed-batch mode (39.9 g/g of dcw)
-
-
?
2-hydroxy-2-phenylacetonitrile + 2 H2O
2-hydroxy-2-phenylacetate + NH3
show the reaction diagram
i.e. (R,S)-mandelonitrile
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
show the reaction diagram
phenylpropionitrile + 2 H2O
phenylpropionate + NH3
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phenylacetonitrile + 2 H2O
phenylacetate + NH3
show the reaction diagram
-
-
-
?
phenylacetonitrile + 2 H2O
phenylacetate + NH3
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.4
2-hydroxy-2-phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme
3.4
phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme
0.8
phenylpropionitrile
pH 8.0, 30°C, recombinant enzyme
11.4
2-hydroxy-2-phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme
3.4
phenylacetonitrile
pH 8.0, 30°C, recombinant enzyme
0.8
phenylpropionitrile
pH 8.0, 30°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
about 45% activity at pH 4.5 compared to the pH optimum at 7.0
5
about 70% activity at pH 5.0 compared to the pH optimum at 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H165N
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
W163A
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
purified recombinant enzyme, room temperature, 2 h, 20% activity remaining
718670
11
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
5.5
purified recombinant enzyme, room temperature, 2 h, 10% activity remaining
718670
6.5
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
7 - 10
purified recombinant enzyme, room temperature, 2 h, 90-100% activity remaining
718670
10.5
purified recombinant enzyme, room temperature, 2 h, 20% activity remaining
718670
11
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
5.5
purified recombinant enzyme, room temperature, 2 h, 10% activity remaining
718670
6.5
purified recombinant enzyme, room temperature, 2 h, 50% activity remaining
718670
7 - 10
purified recombinant enzyme, room temperature, 2 h, 90-100% activity remaining
718670
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 35
purified recombinant enzyme, pH 8.0, 1 h, stable
40
purified recombinant enzyme, pH 8.0, 1 h, 60% activity remaining
45
purified recombinant enzyme, pH 8.0, 1 h, 20% activity remaining
50 - 60
purified recombinant enzyme, pH 8.0, 1 h, about 10% activity remaining
25 - 35
purified recombinant enzyme, pH 8.0, 1 h, stable
40
purified recombinant enzyme, pH 8.0, 1 h, 60% activity remaining
45
purified recombinant enzyme, pH 8.0, 1 h, 20% activity remaining
50 - 60
purified recombinant enzyme, pH 8.0, 1 h, about 10% activity remaining
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 3fold from Escherichia coli strain BL21-Gold(DE3) to near homogeneity
recombinant enzyme 3fold from Escherichia coli strain BL21-Gold(DE3) to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
expression in Escherichia coli strain BL21-Gold (DE3)
expression in Escherichia coli strain BL21-Gold (DE3)
expression ion Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
the enzyme is promising for the enantioretentive transformation of (S)-mandelonitrile
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petrickova, A.; Vesela, A.B.; Kaplan, O.; Kubac, D.; Uhnakova, B.; Malandra, A.; Felsberg, J.; Rinagelova, A.; Weyrauch, P.; K?en, V.; Bezouska, K.; Martinkova, L.
Purification and characterization of heterologously expressed nitrilases from filamentous fungi
Appl. Microbiol. Biotechnol.
93
1553-1561
2012
Aspergillus niger (A2R6M7), Aspergillus niger (A9QXE0), Aspergillus niger CBS 513.88 (A2R6M7), Aspergillus niger CBS 513.88 (A9QXE0), Neurospora crassa, Neurospora crassa OR74A
Manually annotated by BRENDA team
Petrickova, A.; Sosedov, O.; Baum, S.; Stolz, A.; Martinkova, L.
Influence of point mutations near the active site on the catalytic properties of fungal arylacetonitrilases from Aspergillus niger and Neurospora crassa
J. Mol. Catal. B
77
74-80
2012
Aspergillus niger (A2R6M7), Aspergillus niger CBS 513.88 (A2R6M7), Neurospora crassa (V5IPE4), Neurospora crassa DSM 1257 (V5IPE4)
-
Manually annotated by BRENDA team
Vesela, A.; Krenkova, A.; Martinkova, L.
Exploring the potential of fungal arylacetonitrilases in mandelic acid synthesis
Mol. Biotechnol.
57
466-474
2015
Aspergillus niger
-
Manually annotated by BRENDA team