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Information on EC 4.2.1.66 - cyanide hydratase and Organism(s) Microdochium sorghi and UniProt Accession P32964

for references in articles please use BRENDA:EC4.2.1.66
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.66 cyanide hydratase
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This record set is specific for:
Microdochium sorghi
UNIPROT: P32964 not found.
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Word Map
The taxonomic range for the selected organisms is: Microdochium sorghi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
cyanide hydratase, formamide hydrolyase, formamide hydro-lyase, formamide hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CHT
-
-
-
-
formamide dehydratase
formamide hydro-lyase
-
-
formamide hydro-lyase (cyanide-forming)
-
-
formamide hydrolase
-
-
Formamide hydrolyase
-
-
-
-
hydratase, cyanide
-
-
-
-
additional information
-
the enzyme belongs to the nitrilase family of CN hydrolyzing enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formamide = cyanide + H2O
show the reaction diagram
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
formamide hydro-lyase (cyanide-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37292-83-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
HCN + H2O
formamide
show the reaction diagram
HCN + H2O
formamide
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
HCN + H2O
formamide
show the reaction diagram
-
-
-
?
HCN + H2O
formamide
show the reaction diagram
-
HCN is the most effective substrate
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-chloromercuribenzoate
-
-
additional information
-
not inhibited by Ag+, Zn2+, Cu2+, iodoacetamide
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 5.7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
this enzyme participates in cyanoamino acid metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHT_MICSH
368
0
40899
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
300000 - 1000000
gel filtration
40900
x * 40900, calculation from sequence of cDNA
45000
x * 45000, SDS-PAGE
300000 - 1000000
-
gel filtration
40000
-
x * 40000
45000
-
x * 45000, SDS-PAGE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymer
oligomer
-
x * 40000
polymer
-
x * 45000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
N-glycosylation possibly at residue 286-288
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
22 - 24
-
the activity is totally lost by incubation of the mycelia for 16 h at 22-24°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, more than 2 years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, strains and plasmids listed
DNA sequence analysis
-
expression in Escherichia coli BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
searching for enzymes in the bioremediation of cyanide-containing waste
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Bipolaris sorghicola, Colletotrichum graminicola, Colletotrichum magnum, Curvularia lunata, Exserohilum turcicum, Fusarium verticillioides, Macrophomina phaseolina, Microdochium sorghi, Periconia circinata, Stemphylium vesicarium
Manually annotated by BRENDA team
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 oxysporum N-10, Fusarium solani, Fusarium solani IMI 196840, Leptosphaeria maculans, Microdochium sorghi, Stemphylium loti
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Microdochium sorghi (P32964), Microdochium sorghi, Neurospora crassa
Manually annotated by BRENDA team
Gupta, N.; Balomajumder, C.; Agarwal, V.
Enzymatic mechanism and biochemistry for cyanide degradation: A review
J. Hazard. Mater.
176
1-13
2010
Exserohilum turcicum, Fusarium lateritium, Fusarium oxysporum, Fusarium oxysporum CCMI 876, Fusarium solani, Microdochium sorghi, Stemphylium loti
Manually annotated by BRENDA team