Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
acetonitrile + H2O
?
-
-
?
acrylonitrile + H2O
acrylamide
benzonitrile + H2O
?
best substrate for nitrilase activity
-
?
crotononitrile + H2O
crotonic acid amide
methacrylonitrile + H2O
2-methylprop-2-enamide
methacrylonitrile + H2O
?
propionitrile + H2O
?
-
-
?
tetracyanonickelate II + H2O
?
additional information
?
-
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
-
0.76% activity compared to cyanide
-
-
?
2-cyanopyridine + 2 H2O
pyridine 2-carboxylic acid + NH3
-
0.76% activity compared to cyanide
-
-
?
acrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
acrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
acrylonitrile + H2O
acrylamide
-
-
-
-
?
crotononitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
crotononitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
crotononitrile + H2O
crotonic acid amide
-
-
-
-
?
crotononitrile + H2O
crotonic acid amide
-
-
-
-
?
cyanide + H2O
formamide
-
100% activity
-
-
?
cyanide + H2O
formamide
-
100% activity
-
-
?
fumaronitrile + H2O
?
-
0.95% activity compared to cyanide
-
-
?
fumaronitrile + H2O
?
-
0.95% activity compared to cyanide
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
ir
HCN + H2O
formamide
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
-
HCN is the most effective substrate
-
-
r
HCN + H2O
formamide
-
-
-
?
HCN + H2O
formamide
Trichoderma spp.
-
-
-
?
HCN + H2O
formamide
Trichoderma spp.
-
involved in HCN catabolism
-
?
methacrylonitrile + H2O
2-methylprop-2-enamide
-
-
-
-
?
methacrylonitrile + H2O
2-methylprop-2-enamide
-
-
-
-
?
methacrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
methacrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
tetracyanonickelate II + H2O
?
-
-
-
-
?
tetracyanonickelate II + H2O
?
-
-
-
-
?
additional information
?
-
-
almost no activity with benzonitrile, 3-cyanopyridine, 4-cyanopyridine, and phenylacetonitrile
-
-
?
additional information
?
-
-
almost no activity with benzonitrile, 3-cyanopyridine, 4-cyanopyridine, and phenylacetonitrile
-
-
?
additional information
?
-
the enzyme also shows low nitrilase activity, which is sufficient for the fungus to grow on acetonitrile, propionitrile, or benzonitrile as sole nitrogen source
-
?
additional information
?
-
-
the enzyme also shows low nitrilase activity, which is sufficient for the fungus to grow on acetonitrile, propionitrile, or benzonitrile as sole nitrogen source
-
?
additional information
?
-
-
low hydrolytic activity with a metal-cyano complex, tetracyanonickelate, the enzyme also shows nitrilase activity
-
?
additional information
?
-
-
low hydrolytic activity with a metal-cyano complex, tetracyanonickelate, the enzyme also shows nitrilase activity
-
?
additional information
?
-
-
hydrolysis of a metal-cyano complex, tetracyanonickelate
-
?
additional information
?
-
-
hydrolysis of a metal-cyano complex, tetracyanonickelate
-
?
additional information
?
-
-
hydrolysis of a metal-cyano complex, tetracyanonickelate
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
comparison of fungal nitrilases to determine best candidates for the remediation of cyanide-containing industrial wastewater, enzyme of Aspergillus nidulans indicates highest reaction rate of the four fungal nitrilases compared in the study
additional information
-
comparison of fungal nitrilases to determine best candidates for the remediation of cyanide-containing industrial wastewater, analysis according to relative specific activity, pH activity profile, thermal stability, and ability to remediate cyanide contaminated waste water from silver and copper electroplating baths
additional information
cyanide hydratase and nitrilase activity
additional information
-
cyanide hydratase and nitrilase activity
additional information
comparison of fungal nitrilases to determine best candidates for the remediation of cyanide-containing industrial wastewater, lowest activity of the group of nitrilases compared in this study, does not reach maximum activity until 80 mM KCN
additional information
-
comparison of fungal nitrilases to determine best candidates for the remediation of cyanide-containing industrial wastewater, lowest activity of the group of nitrilases compared in this study, does not reach maximum activity until 80 mM KCN
additional information
-
comparison of fungal nitrilases to determine best candidates for the remediation of cyanide-containing industrial wastewater, most promising candidate isolated from Neurospora crassa, according to high activity over a wide range of pH values, stability for at least 48 h when incubated at temperatures ranging from 27°C to 43°C, highest rates at a substrate concentration of 20 mM KCN, maximal rates around 60 mM KCN
additional information
-
three-dimensional protein reconstruction, negative stain electron microscopy, three-dimensional reconstruction, comparative modeling and docking, recombinant cyanide hydratase fibers analyzed by iterative helical real space reconstruction, determination of left-handed D1 S5.4 symmetry with helical rise of 1.36 nm, different arrangement from other microbial nitrilases that display a reduced helical twist, assembly stabilized by two dyadic interactions between dimers across the one-start helical groove, stereoview of the docked model
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K136R/D275E/V281A/M302S
mutant enzyme shows lower activity
T12Q/S13A
mutant enzyme shows lower activity
D275E
-
site-directed mutagenesis, 0-29% reduced activity compared to the wild-type enzyme
D275E
site-directed mutagenesis, 0-29% reduced activity compared to the wild-type enzyme
F170L
no activity
F170L
-
site-directed mutagenesis, inactive mutant compared to the wild-type enzyme
F170L
site-directed mutagenesis, inactive mutant compared to the wild-type enzyme
K136R
-
site-directed mutagenesis, 52% reduced activity compared to the wild-type enzyme
K136R
site-directed mutagenesis, 52% reduced activity compared to the wild-type enzyme
M302S
-
site-directed mutagenesis, 22% reduced activity compared to the wild-type enzyme
M302S
site-directed mutagenesis, 22% reduced activity compared to the wild-type enzyme
S13A
-
site-directed mutagenesis, 19-47% reduced activity compared to the wild-type enzyme
S13A
site-directed mutagenesis, 19-47% reduced activity compared to the wild-type enzyme
T12P
-
site-directed mutagenesis, inactive mutant
T12P
site-directed mutagenesis, inactive mutant
T12Q
-
site-directed mutagenesis, 10-48% reduced activity compared to the wild-type enzyme
T12Q
site-directed mutagenesis, 10-48% reduced activity compared to the wild-type enzyme
V281A
-
site-directed mutagenesis, 8% reduced activity compared to the wild-type enzyme
V281A
site-directed mutagenesis, 8% reduced activity compared to the wild-type enzyme
additional information
-
REMI technique is used to construct mutants with improved cyanide-degradation ability from biocontrol fungus Trichoderma koningii strain T30. Transformants TkA9 (0.00553 mM formamide formed per h and mg protein) from T30 and Th64 (5.35 mM formamide formed per h and mg protein) from T21 had higher cyanide hydratase activity than other transformants and their wild strains
additional information
-
REMI technique is used to construct mutants with improved cyanide-degradation ability from biocontrol fungus Trichoderma koningii strain T30. Transformants TkA9 (0.00553 mM formamide formed per h and mg protein) from T30 and Th64 (5.35 mM formamide formed per h and mg protein) from T21 had higher cyanide hydratase activity than other transformants and their wild strains
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fry, W.E.; Millar, R.L.
Cyanide degradion by an enzyme from Stemphylium loti
Arch. Biochem. Biophys.
151
468-474
1972
Stemphylium loti
brenda
Nazly, N.; Knowles, C.J.
Cyanide degradation by immobilised fungi
Biotechnol. Lett.
3
363-368
1981
Stemphylium loti
-
brenda
Miller, J.; Conn, E.E.
Metabolism of hydrogen cyanide by higher plants
Plant Physiol.
65
1199-1202
1980
Microdochium sorghi, no activity in higher plants
brenda
Wang, P.; VanEtten, H.D.
Cloning and properties of a cyanide hydratase gene from the phytopathogenic fungus Gloeocercospora sorghi
Biochem. Biophys. Res. Commun.
187
1048-1054
1992
Colletotrichum graminicola, Microdochium sorghi (P32964), Microdochium sorghi
brenda
Wang, P.; Matthews, D.E.; VanEtten, H.D.
Purification and characterization of cyanide hydratase from the phytopathogenic fungus Gloeocercospora sorghi
Arch. Biochem. Biophys.
298
569-575
1992
Aspergillus nidulans, Colletotrichum graminicola, Colletotrichum magnum, Curvularia lunata, Fusarium verticillioides, Microdochium sorghi, Bipolaris sorghicola, Exserohilum turcicum, Macrophomina phaseolina, Periconia circinata, Stemphylium vesicarium
brenda
Cluness, M.J.; Turner, P.; Clements, E.; Brown, D.T.; O'Reilly, C.
Purification and properties of cyanide hydratase from Fusarium lateritium and analysis of the corresponding chy1 gene
J. Gen. Microbiol.
139
1807-1815
1993
Fusarium lateritium
brenda
Brown, D.T.; Turner, P.D.; O'Reilly, C.
Expression of the cyanide hydratase enzyme from Fusarium lateritium in Escherichia coli and identification of an essential cysteine residue
FEMS Microbiol. Lett.
134
143-146
1995
Fusarium lateritium
brenda
Ezzi, M.I.; Lynch, J.M.
Cyanide catabolizing enzymes in Trichoderma spp.
Enzyme Microb. Technol.
31
1042-1047
2002
Trichoderma spp.
-
brenda
Nolan, L.M.; Harnedy, P.A.; Turner, P.; Hearne, A.B.; O'Reilly, C.
The cyanide hydratase enzyme of Fusarium lateritium also has nitrilase activity
FEMS Microbiol. Lett.
221
161-165
2003
Fusarium lateritium (P32963), Fusarium lateritium
brenda
O'Reilly, C.; Turner, P.D.
The nitrilase family of CN hydrolyzing enzymes - a comparative study
J. Appl. Microbiol.
95
1161-1174
2003
Fusarium lateritium, Fusarium oxysporum, Fusarium solani, Microdochium sorghi, Leptosphaeria maculans, Stemphylium loti, Fusarium solani IMI 196840, Fusarium oxysporum N-10
brenda
Mak, K.K.W.; Yanase, H.; Renneberg, R.
Novel optical biotest for determination of cyanide traces in marine fish using microbial cyanide hydratase and formate dehydrogenase
Microchim. Acta
149
131-135
2005
Fusarium oxysporum
-
brenda
Zhou, X.; Xu, S.; Liu, L.; Chen, J.
Degradation of cyanide by Trichoderma mutants constructed by restriction enzyme mediated integration (REMI)
Biores. Technol.
98
2958-2962
2007
Trichoderma koningii, Trichoderma koningii T30
brenda
Woodward, J.D.; Weber, B.W.; Scheffer, M.P.; Benedik, M.J.; Hoenger, A.; Sewell, B.T.
Helical structure of unidirectionally shadowed metal replicas of cyanide hydratase from Gloeocercospora sorghi
J. Struct. Biol.
161
111-119
2007
Microdochium sorghi
brenda
Basile, L.J.; Willson, R.C.; Sewell, B.T.; Benedik, M.J.
Genome mining of cyanide-degrading nitrilases from filamentous fungi
Appl. Microbiol. Biotechnol.
80
427-435
2008
Aspergillus nidulans, Fusarium graminearum, Neurospora crassa, Microdochium sorghi (P32964), Microdochium sorghi
brenda
Dent, K.C.; Weber, B.W.; Benedik, M.J.; Sewell, B.T.
The cyanide hydratase from Neurospora crassa forms a helix which has a dimeric repeat
Appl. Microbiol. Biotechnol.
82
271-278
2009
Neurospora crassa
brenda
Gupta, N.; Balomajumder, C.; Agarwal, V.
Enzymatic mechanism and biochemistry for cyanide degradation: A review
J. Hazard. Mater.
176
1-13
2010
Fusarium lateritium, Fusarium oxysporum, Fusarium solani, Microdochium sorghi, Exserohilum turcicum, Stemphylium loti, Fusarium oxysporum CCMI 876
brenda
Wang, S.; Liu, Y.; Li, Q.; Tong, Z.; Qin, Y.; Xu, J.
Analysis of cyanide-degrading metabolism and optimization of culture condition for cyanide-degrading enzyme production from Alcaligenes sp. DN25
Huagong Xuebao
62
482-489
2011
Alcaligenes sp., Alcaligenes sp. DN25
-
brenda
Rinagelov, A.; Kaplan, O.; Vesela, A.; Chmatal, M.; Krenkova, A.; Plihal, O.; Pasquarelli, F.; Cantarella, M.; Martinkov, L.
Cyanide hydratase from Aspergillus niger K10: Overproduction in Escherichia coli, purification, characterization and use in continuous cyanide degradation
Process Biochem.
49
445-450
2014
Aspergillus niger, Aspergillus niger K-10
-
brenda
Martinkova, L.; Vesela, A.B.; Rinagelova, A.; Chmatal, M.
Cyanide hydratases and cyanide dihydratases emerging tools in the biodegradation and biodetection of cyanide
Appl. Microbiol. Biotechnol.
99
8875-8882
2015
Fusarium lateritium (P32963)
brenda
Kushwaha, M.; Kumar, V.; Mahajan, R.; Bhalla, T.C.; Chatterjee, S.; Akhter, Y.
Molecular insights into the activity and mechanism of cyanide hydratase enzyme associated with cyanide biodegradation by Serratia marcescens
Arch. Microbiol.
200
971-977
2018
Serratia marcescens, Serratia marcescens WW4
brenda
Martinkova, L.; Chmatal, M.
The integration of cyanide hydratase and tyrosinase catalysts enables effective degradation of cyanide and phenol in coking wastewaters
Water Res.
102
90-95
2016
Aspergillus niger (A9QXE0), Aspergillus niger K10 (A9QXE0)
brenda