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 A9QXE0

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: A9QXE0
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
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
-
-
-
?
(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
-
-
?
(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
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHT_ASPNG
356
0
40022
Swiss-Prot
-
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
expression in Escherichia coli strain BL21-Gold (DE3)
expressed in Escherichia coli JM109 cells
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