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Information on EC 3.5.5.4 - cyanoalanine nitrilase
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EC Tree
3.5.5.4 cyanoalanine nitrilaseIUBMB Comments
L-Asparagine is formed as an intermediate. cf. EC 4.2.1.65, 3-cyanoalanine hydratase and EC 3.5.1.1, asparaginase.
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Word Map
- 3.5.5.4
-
cyanogenic
- hcn
- degradation
- brassicaceae
- ethylene
- sorghum
-
volatile
- glucosinolates
- glycoside
-
cyanide-containing
-
pseudoalcaligenes
- waste
-
biodegradation
- bicolor
-
cyanide-resistance
- ammonia
- dhurrin
- auxin
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-cyanoalanine nitrilase, beta-cyanoalanine nitrilase, beta-cyanoalanine synthase, cyanoalanine hydratase, NIT-T4, NIT1, NIT2, Nit4, NIT4-1, NIT4-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-cyanoalanine nitrilase
beta-cyanoalanine nitrilase
beta-cyanoalanine synthase
Nit4
NIT4-1
NIT4-2
NIT4A
NIT4B
nitrilase 4
PinA
beta-cyanoalanine nitrilase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-cyano-L-alanine + 2 H2O = L-aspartate + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of nitriles
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
3-cyano-L-alanine aminohydrolase
L-Asparagine is formed as an intermediate. cf. EC 4.2.1.65, 3-cyanoalanine hydratase and EC 3.5.1.1, asparaginase.
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CAS REGISTRY NUMBER
COMMENTARY
85638-44-4
-
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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
phenyl-3-propionitrile + H2O
phenyl-3-propionic acid + NH3
-
-
-
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
enzyme has additional hydratase activity for 3-cyano-L-alanine, ratio of hydratase activity to nitrilase activity is 3.3:1. L-asparagine and L-aspartate are formed at the same time, asparagine is not an intermediate
-
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
enzyme has additional hydratase activity for 3-cyano-L-alanine, ratio of hydratase activity to nitrilase activity is 4:1. L-asparagine and L-aspartate are formed at the same time, asparagine is not an intermediate
-
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
-
L-asparagine is formed as an intermediate
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
-
L-asparagine is formed as an intermediate
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
high activity substrate for isozyme complexes NIT4A/B2 and NIT4A/B1
-
-
ir
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
the reaction is catalyzed only by isoform NIT4A, L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
the reaction is catalyzed only by isoform NIT4A, L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
beta-cyano-L-alanine + H2O
L-aspartate + NH3
-
L-asparagine is formed as an intermediate
-
-
?
additional information
?
-
-
indole-3-acetonitrile is no substrate for NIT-T4
-
-
?
additional information
?
-
-
isoform NIT4B does not show beta-cyano-L-alanine-hydrolyzing activity
-
-
?
additional information
?
-
no substrate: indole-3-acetonitrile
-
-
?
additional information
?
-
no substrate: indole-3-acetonitrile
-
-
?
additional information
?
-
-
no substrates are various nitrile or amide compounds, overview
-
-
?
additional information
?
-
-
no substrates are various nitrile or amide compounds, overview
-
-
?
additional information
?
-
-
recombinant NIT4 isozymes NIT4A, NIT4B1, and NIT4B2 do not hydrolyze 3-cyano-L-alanine, benzonitrile, 4-hydroxybenzonitrile, butyronitrile, and 4-pentenenitrile
-
-
?
additional information
?
-
-
isoform NIT4B1 does not show any beta-cyano-L-alanine-hydrolyzing activity
-
-
?
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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
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
-
L-asparagine is formed as an intermediate
?
3-cyano-L-alanine + H2O
L-aspartate + NH3
-
-
L-asparagine is formed as an intermediate
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.69
3-Cyano-L-alanine
-
in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
0.86
3-Cyano-L-alanine
-
isozyme complex NIT4A/B1, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C
0.89
3-Cyano-L-alanine
-
isozyme complex NIT4A/B2, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.4
3-Cyano-L-alanine
-
in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform LaNIT4A, in addition to nitrilase activity, enzyme shows cyanoalanine hydratase activity
SwissProt
brenda
isoform LaNIT4B, in addition to nitrilase activity, enzyme shows cyanoalanine hydratase activity
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
-
increased expression of beta-cyanoalanine nitrilase improves cyanide tolerance in Arabidopsis thaliana
malfunction
-
the NIT4 deletion shows decreased growth along with altered chlorophyll content under water deficit as compared to the wild type
malfunction
a nit4 knockout mutant of Pseudomonas pseudoalcaligenes CECT 5344 becomes severely impaired in its ability to grow with 3-cyanoalanine and cyanide as nitrogen sources
malfunction
Pseudomonas oleovorans CECT 5344
-
a nit4 knockout mutant of Pseudomonas pseudoalcaligenes CECT 5344 becomes severely impaired in its ability to grow with 3-cyanoalanine and cyanide as nitrogen sources
-
metabolism
the gene cluster including cio1 and nit4 could be involved both in cyanide resistance and in its assimilation by Pseudomonas pseudoalcaligenes CECT 5344
metabolism
Pseudomonas oleovorans CECT 5344
-
the gene cluster including cio1 and nit4 could be involved both in cyanide resistance and in its assimilation by Pseudomonas pseudoalcaligenes CECT 5344
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NRL4A_LUPAN
349
0
37762
Swiss-Prot
other Location (Reliability: 3)
NRL4A_TOBAC
349
0
37555
Swiss-Prot
other Location (Reliability: 3)
NRL4B_LUPAN
350
0
38055
Swiss-Prot
other Location (Reliability: 2)
NRL4B_TOBAC
348
0
37534
Swiss-Prot
other Location (Reliability: 3)
NRL4_ARATH
355
0
38895
Swiss-Prot
other Location (Reliability: 3)
NRL4_ORYSJ
362
0
38676
Swiss-Prot
other Location (Reliability: 3)
K0KKW9_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
304
0
33351
TrEMBL
other Location (Reliability: 2)
A0A067Z3P3_GLUOY
321
0
35085
TrEMBL
-
A0A3B0R8Y0_9ZZZZ
161
0
18232
TrEMBL
other Location (Reliability: 2)
A0A396I498_MEDTR
205
0
22701
TrEMBL
other Location (Reliability: 2)
A0A212KM05_9PROT
311
0
33250
TrEMBL
-
A0A396IC97_MEDTR
125
0
13487
TrEMBL
other Location (Reliability: 5)
A0A212IW40_9DELT
315
0
34524
TrEMBL
-
A0A0B6AAE0_BACMB
Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / VKM B-512)
318
0
35116
TrEMBL
-
A0A3B0RGR6_9ZZZZ
311
0
33930
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2I0A9E6_9ASPA
351
0
37737
TrEMBL
other Location (Reliability: 4)
A0A2G9HT68_9LAMI
233
0
25494
TrEMBL
other Location (Reliability: 4)
F0Q9A2_ACIAP
Acidovorax avenae (strain ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011)
316
0
33638
TrEMBL
-
A0A251SW76_HELAN
344
0
37072
TrEMBL
other Location (Reliability: 3)
A0A072UKA3_MEDTR
350
0
37868
TrEMBL
other Location (Reliability: 2)
A0A6J4JBT1_9ACTN
325
0
34960
TrEMBL
-
A0A6J4UTC9_9CHLR
312
0
33376
TrEMBL
-
A0A251VDZ8_HELAN
344
0
37140
TrEMBL
other Location (Reliability: 2)
W6R265_PSEP5
Pseudomonas pseudoalcaligenes (strain CECT 5344)
324
0
35380
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
polymer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
PinA is able to complement a nit4 mutation in Arabidopsis thaliana. Overexpression of PinA in wild-type Arabidopsis thaliana results in increased growth in high concentrations of 3-cyano-L-alanine and in increased root elongation in the absence of exogenous 3-cyano-L-alanine
additional information
-
PinA is able to complement a nit4 mutation in Arabidopsis thaliana. Overexpression of PinA in wild-type Arabidopsis thaliana results in increased growth in high concentrations of 3-cyano-L-alanine and in increased root elongation in the absence of exogenous 3-cyano-L-alanine
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose Fast Flow column chromatography and Sephadex G-15 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli enables the recombinant strain to fully assimilate 3-cyanoalanine
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cyanide as a sole nitrogen source induces activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
-
this enzyme is of interest for the use in the biodegradation of cyanide and the degradation of nitrile wastes
degradation
-
this enzyme is of interest for the use in the biodegradation of cyanide and the degradation of nitrile wastes
degradation
-
this enzyme is of interest for the use in the biodegradation of cyanide and the degradation of nitrile wastes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yanase, H.; Sakai, T.; Tonomura, K.
Metabolism of nitriles in microorganisms. Part V. Purification, crystallization and some properties of beta-cyano-L-alanine-degrading enzyme in Pseudomonas sp. 13
Agric. Biol. Chem.
47
473-482
1983
Pseudomonas sp., Pseudomonas sp. 13
-
brenda
Piotrowski, M.; Volmer, J.J.
Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4 homolog
Plant Mol. Biol.
61
111-122
2006
Lupinus angustifolius (Q3LRV4), Lupinus angustifolius (Q5QGZ8)
brenda
Kriechbaumer, V.; Park, W.J.; Piotrowski, M.; Meeley, R.B.; Gierl, A.; Glawischnig, E.
Maize nitrilases have a dual role in auxin homeostasis and beta-cyanoalanine hydrolysis
J. Exp. Bot.
58
4225-4233
2007
Zea mays
brenda
Ishikawa, T.; Okazaki, K.; Kuroda, H.; Itoh, K.; Mitsui, T.; Hori, H.
Molecular cloning of Brassica rapa nitrilases and their expression during clubroot development
Mol. Plant Pathol.
8
623-637
2007
Brassica rapa
brenda
Jenrich, R.; Trompetter, I.; Bak, S.; Olsen, C.E.; Moller, B.L.; Piotrowski, M.
Evolution of heteromeric nitrilase complexes in Poaceae with new functions in nitrile metabolism
Proc. Natl. Acad. Sci. USA
104
18848-18853
2007
Sorghum bicolor
brenda
Howden, A.J.; Harrison, C.J.; Preston, G.M.
A conserved mechanism for nitrile metabolism in bacteria and plants
Plant J.
57
243-253
2009
Pseudomonas fluorescens, Pseudomonas fluorescens SBW25
brenda
Gupta, N.; Balomajumder, C.; Agarwal, V.
Enzymatic mechanism and biochemistry for cyanide degradation: A review
J. Hazard. Mater.
176
1-13
2010
Priestia megaterium, Chromobacterium violaceum, Escherichia coli
brenda
Janowitz, T.; Trompetter, I.; Piotrowski, M.
Evolution of nitrilases in glucosinolate-containing plants
Phytochemistry
70
1680-1686
2009
Allium cepa, Arabidopsis thaliana, Brassica rapa, Carica papaya, Ricinus communis, Glycine max, Hordeum vulgare, Lactuca sativa, Linum usitatissimum, Lotus japonicus, Lupinus angustifolius, Solanum lycopersicum, Manihot esculenta, Medicago truncatula, Mesembryanthemum crystallinum, Nicotiana tabacum, Oryza sativa, Physcomitrium patens, Pinus taeda, Populus trichocarpa, Saccharum officinarum, Sorghum bicolor, Triticum aestivum, Tropaeolum majus, Vitis vinifera, Zea mays, Curcuma longa, Selaginella moellendorffii, Capsella rubella, Tarenaya spinosa
brenda
O'Leary, B.; Preston, G.M.; Sweetlove, L.J.
Increased beta-cyanoalanine nitrilase activity improves cyanide tolerance and assimilation in Arabidopsis
Mol. Plant
7
231-243
2014
Pseudomonas fluorescens
brenda
Machingura, M.; Sidibe, A.; Wood, A.J.; Ebbs, S.D.
The beta-cyanoalanine pathway is involved in the response to water deficit in Arabidopsis thaliana
Plant Physiol. Biochem.
63
159-169
2013
Arabidopsis thaliana
brenda
Acera, F.; Carmona, M.I.; Castillo, F.; Quesada, A.; Blasco, R.
A cyanide-induced 3-cyanoalanine nitrilase in the cyanide-assimilating bacterium Pseudomonas pseudoalcaligenes strain CECT 5344
Appl. Environ. Microbiol.
83
e00089-17
2017
Pseudomonas oleovorans (W6R265), Pseudomonas oleovorans CECT 5344 (W6R265)
brenda
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