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Information on EC 4.2.1.66 - cyanide hydratase
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EC Tree
4.2.1.66 cyanide hydrataseSpecify your search results
Word Map
- 4.2.1.66
- nitrilase
-
cyanogenic
-
fusarium
- sorghi
- lateritium
-
cyanide-degrading
- hcn
-
nitril
-
dihydratase
- biotechnology
- stutzeri
- analysis
- environmental protection
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cyanide hydratase, formamide hydro-lyase, formamide hydrolyase, formamide hydrolase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CHT
formamide dehydratase
formamide hydro-lyase
formamide hydro-lyase (cyanide-forming)
formamide hydrolase
Formamide hydrolyase
-
-
-
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hydratase, cyanide
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-
-
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NitAn1
additional information
CHT
-
-
-
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formamide dehydratase
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-
-
-
additional information
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the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
-
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
-
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
-
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
additional information
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the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formamide = cyanide + H2O
reaction proceeds irreversibly in opposite direction
-
formamide = cyanide + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
formamide hydro-lyase (cyanide-forming)
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CAS REGISTRY NUMBER
COMMENTARY
37292-83-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzonitrile + H2O
?
best substrate for nitrilase activity
-
?
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
-
?
crotononitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
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-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
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-
?
HCN + H2O
formamide
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
HCN + H2O
formamide
-
emediation of cyanide-containing industrial wastewater analyzed
-
-
?
methacrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
methacrylonitrile + H2O
?
-
about 0.05% of the activity with HCN
-
?
additional information
?
-
-
almost no activity with benzonitrile, 3-cyanopyridine, 4-cyanopyridine, and phenylacetonitrile
-
-
?
additional information
?
-
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almost no activity with benzonitrile, 3-cyanopyridine, 4-cyanopyridine, and phenylacetonitrile
-
-
?
additional information
?
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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
?
-
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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
?
-
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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
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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rate of the reaction decreases at high substrate concentrations, indicative of substrate inhibition
-
additional information
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not inhibited by Ag+, Zn2+, Cu2+, iodoacetamide
-
additional information
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rate of the reaction decreases at high substrate concentrations, indicative of substrate inhibition
-
additional information
-
EDTA, ammonium chloride, potassium chloride, magnesium chloride or calcium chloride do not inhibit the enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Trichoderma spp.
-
no induction of enzyme expression by cyanide in the different strains
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Mycoses
Cloning and properties of a cyanide hydratase gene from the phytopathogenic fungus Gloeocercospora sorghi.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 9
6 - 8.5
5.2 - 9
-
relatively wide range of >50% activity relative to its maximal rate
5.2 - 9
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at least half-maximal activity between pH 5.2 and pH 9, widest range of activity in comparison to four other enzymes used in this study
6 - 8.5
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at least half-maximal activity between approximately pH 6 and pH 8.5, narrower range of activity in comparison to four other enzymes used in this study
6 - 8.5
narrow range of activity in comparison to four other enzymes used in this study, more tolerant of higher than of lower pH values
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27 - 50
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incubated at 27°C, 37°C, 43°C, and 50°C, activity measured at time points ranging between 0 and 48 h, at 37°C and 43°C most stable with no loss of activity after 48 h at 37°C, about 40% of activity remaining after 48 h at 43°C, at 50°C activity below 5% by 48 h
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Trichoderma spp.
several strains with varying levels of enzyme activity, constitutive expression of the gene encoding the enzyme
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
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cyanide degradation is performed by co-functioning of the cyanide hydratase, an amidase, and a cyanide hydrolase, overview
metabolism
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cyanide degradation is performed by co-functioning of the cyanide hydratase, an amidase, and a cyanide hydrolase, overview
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Show AA Sequence and Transmembrane Helices (415 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
300000
300000 - 1000000
40000
45000
additional information
-
the helical structure of cyanide hydratase is determined at a resolution of about 33 A by applying the iterative helical real-space reconstruction method algorithm to freeze-dried unidirectionally shadowed filaments. These filaments are left-handed
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
polymer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
N-glycosylation possibly at residue 286-288
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D275E
F170L
K136R
M302S
S13A
T12P
T12Q
V281A
additional information
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
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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
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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 24
-
the activity is totally lost by incubation of the mycelia for 16 h at 22-24°C
27 - 50
28 - 55
-
the enzyme shows a half-life of 5.6 hat 28°C and is unstable at temperatures above 35°C. The enzyme is still active at 50°C with ca. 36% of its maximum activity, but nearly inactive at 55°C
27 - 50
-
incubated at 27°C, 37°C, 43°C, and 50°C, activity measured at time points ranging between 0 and 48 h, enzyme of Aspergillus nidulans quickly looses activity at the two highest temperatures, and 50% of activity is lost after 48 h at 37°C
27 - 50
-
incubated at 27°C, 37°C, 43°C, and 50°C, activity measured at time points ranging between 0 and 48 h, CHT of Gibberella zeae shows an initial increase in activity at lower temperatures, subsequent stability is similar to that of Neurospora crassa, gradual decrease in activity at 50°C
27 - 50
incubated at 27°C, 37°C, 43°C, and 50°C, activity measured at time points ranging between 0 and 48 h, enzyme quickly looses activity at the two highest temperatures, 50% of activity is lost after 48 h at 37°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Hi-Prep 16/10 Q FF column chromatography and Sephacryl S-200 gel filtration
-
recombinant protein, gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence analysis
expressed in Escherichia coli, pET26b construct p3460, BL21(lambda-DE3) pLysS cells
-
expressed in Escherichia coli, strains and plasmids listed
overexpression of the wild-type and mutant enzymes in Escherichia coli XL1-Blue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
environmental protection
additional information
analysis
-
optical biotest for determination of cyanide traces in marine fish using microbial cyanide hydratase and formate dehydrogenase
biotechnology
-
searching for enzymes in the bioremediation of cyanide-containing waste
biotechnology
-
searching for enzymes in the bioremediation of cyanide-containing waste
biotechnology
-
searching for enzymes in the bioremediation of cyanide-containing waste
biotechnology
searching for enzymes in the bioremediation of cyanide-containing waste
environmental protection
the integration of cyanide hydratase and tyrosinase open up new possibilities for the bioremediation of wastewaters with complex pollution. Almost full degradation of free cyanide in the model and the real coking wastewaters is achieved by using a recombinant cyanide hydratase in the first step. The removal of cyanide, a strong inhibitor of tyrosinase, enables an effective degradation of phenols by this enzyme in the second step. Phenol is completely removed from a real coking wastewater within 20 h and cresols are removed by 66% under the same conditions
environmental protection
-
the integration of cyanide hydratase and tyrosinase open up new possibilities for the bioremediation of wastewaters with complex pollution. Almost full degradation of free cyanide in the model and the real coking wastewaters is achieved by using a recombinant cyanide hydratase in the first step. The removal of cyanide, a strong inhibitor of tyrosinase, enables an effective degradation of phenols by this enzyme in the second step. Phenol is completely removed from a real coking wastewater within 20 h and cresols are removed by 66% under the same conditions
-
additional information
-
strain DN25 shows high cyanide degradation activity and has a potential of industiral application
additional information
-
strain DN25 shows high cyanide degradation activity and has a potential of industiral application
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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