EC Number   |
Recommended Name |
Application |
|---|
   3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
strain ADP, use of atrazine as sole nitrogen source, but not as sole carbon source. Comparison of degradation products with those from Pseudoaminobacter sp. and Nocardiodes sp. |
| 3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
use of atrazine as sole nitrogen source and as sole carbon source. Comparison of degradation products with those from Pseudomonas sp. and Nocardiodes sp. |
| 3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
use of atrazine as sole nitrogen source and as sole carbon source. End product of atrazine metabolism is N-ethylammelide. Comparison of degradation products with those from Pseudomonas sp. and Nocardiodes sp. |
| 3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
mineralization of low concentrations of atrazine in the groundwater zone at low temperatures is possible by bioremediation treatments. In combined biostimulation treatment using citrate or molasses and augmentation with Pseudomonas citronellolis ADP or Arthrobacter aurescens strain TC1, up to 76% of atrazine is mineralized at 30°C, and the atrazine degradation gene numbers increase up to 10 million copies/g soil |
| 3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
mineralization of low concentrations of atrazine in the groundwater zone at low temperatures is possible by bioremediation treatments. In combined biostimulation treatment using citrate or molasses and augmentation with Pseudomonas citronellolis ADP or Arthrobacter aurescens strain TC1, up to 76%of atrazine is mineralized at 30°C, and the atrazine degradation gene numbers increase up to 10 million copies/g soil |
| 3.5.4.43 | hydroxydechloroatrazine ethylaminohydrolase |
degradation |
strain HB-6 is capable of utilizing atrazine and cyanuric acid as a sole nitrogen source for growth and even cleaves the s-triazine ring and mineralizes atrazine. The strain demonstrate a very high efficiency of atrazine biodegradation with a broad optimum pH and temperature ranges and can be enhanced by cooperating with other bacteria |
 3.5.5.4 | cyanoalanine nitrilase |
degradation |
this enzyme is of interest for the use in the biodegradation of cyanide and the degradation of nitrile wastes |
| 3.5.99.5 | 2-aminomuconate deaminase |
degradation |
new tryptophan catabolic pathway in Burholderia cepacia J2315, formation of the intermediate 4-oxalocrotonate differentiates this pathway from the proposed mammalian pathway which converts 2-aminomuconate to 2-ketoadipate and, ultimately, glutaryl-coenzyme A |
| 3.7.1.2 | fumarylacetoacetase |
degradation |
the enzyme is part of the key catabolic trait for biodegradation of a small number of aromatic compounds |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
degradation |
key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders |
| 3.7.1.11 | cyclohexane-1,2-dione hydrolase |
degradation |
the enzyme is involved in biodegradation of alicyclic compounds involving a C-C bond ring cleavage to generate an aliphatic intermediate. Alicyclic alcohols compounds, which can serve as insecticides, herbicides, or as intermediates and solvents in chemical industries, are widespread in nature as the secondary metabolites of plant and occurring in fossil fuels |
| 3.8.1.3 | haloacetate dehalogenase |
degradation |
the enzyme has a great potential in lowing its energy barrier toward efluorination of per- or polyfluoropropionic acids. Future in silico and in vitro efforts focusing on the directed mutations and enzyme engineering are required to enable its efficient degradation toward perfluorocarboxylic acids |
| 3.8.1.5 | haloalkane dehalogenase |
degradation |
simple route of detoxification |
| 3.8.1.5 | haloalkane dehalogenase |
degradation |
potential biocatalyst for bioremediation/biosensing of mixed pollutants |
| 4.1.1.2 | oxalate decarboxylase |
degradation |
oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid |
| 4.1.1.102 | phenacrylate decarboxylase |
degradation |
expression of aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2 increases conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Combined overexpression of ALD5, PAD1, ATF1 and ATF2 helps Saccharomyces cerevisiae in phenolics conversion and tolerance |
| 4.1.99.2 | tyrosine phenol-lyase |
degradation |
removal and bioconversion of phenol in wastewater by a thermostable beta-tyrosinase |
| 4.2.1.28 | propanediol dehydratase |
degradation |
possible use in anaerobic polyethylene glycol degradation |
| 4.2.1.84 | nitrile hydratase |
degradation |
treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M |
| 4.2.1.84 | nitrile hydratase |
degradation |
treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M |
| 4.2.2.1 | hyaluronate lyase |
degradation |
use of biocompatible magnetic macroporous bead cellulose functionalised with hyaluronan lyase for controlled fragmetation of hyaluronan. Immobilisation of enzyme on macroporous bead cellulose via reductive amination or macroporous bead cellulose with fixed iminodiacetic acid via a His8-tag has minimal impact on its catalytic activity. The carrier with with fixed iminodiacetic acid shows excellent operational and storage stability, and both carriers enable reproducible time-controlled fragmentation of highly viscous high moleculare weight hyaluronan solutions, yielding hyaluronan fragments of appropriate molecular weight |
| 4.2.2.2 | pectate lyase |
degradation |
useful for degradation of pectin networks at high temperatures |
| 4.2.2.2 | pectate lyase |
degradation |
enzyme is able to remove most of pectin in hemp fiber with less damage compared to alkaline degumming. Predigestion with the enzyme improves glucose and xylose yield by 14.2% and 311.6%, respectively, for corn stalk, 6.5% and 55% for rice stalk compared with sole action of Novozymes Cellic CTec2 |
| 4.2.2.2 | pectate lyase |
degradation |
significant ramie (Boehmeria nivea) fiber weight loss (21.5%) is obtained following enzyme treatment and combined enzyme-chemical treatment (29.3%). The productivity may reach 48.3 U ml/h under high-cell-density cultivation for 30 h in 1l fed-batch fermenter, using Escherichia coli as host |
| 4.2.2.3 | mannuronate-specific alginate lyase |
degradation |
alginate lyase is probably not suitable for hydrolysis of microcapsules in the presence of cells, in order to achieve high cell density and high productivity. However, the high activity may be useful for releasing cells from alginate beads or AG/PLL microcapsules |
| 4.2.2.3 | mannuronate-specific alginate lyase |
degradation |
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata |
| 4.2.2.3 | mannuronate-specific alginate lyase |
degradation |
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields |
| 4.2.2.11 | guluronate-specific alginate lyase |
degradation |
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata |
| 4.2.2.11 | guluronate-specific alginate lyase |
degradation |
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields |
| 4.2.2.26 | oligo-alginate lyase |
degradation |
combining exotype alginate lyases OalC6 and OalC17 and the endotype alginate lyase AlySY08 enables the production of alginate monomers due to synergistic processes |
| 4.2.2.26 | oligo-alginate lyase |
degradation |
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields |
| 4.3.1.18 | D-Serine ammonia-lyase |
degradation |
the enzyme is applied to remove endogenous D-serine from organotypic hippocampal slices. Complete removal of D-serine virtually abolishes NMDA-elicited neurotoxicity |
| 4.4.1.16 | selenocysteine lyase |
degradation |
transgenic plants could be used for decontamination of high Se soil or water |
| 4.4.1.23 | 2-hydroxypropyl-CoM lyase |
degradation |
the phylotype Nocardioides (Actinobacteria) is responsible for carbon assimilation from vinyl chloride. This phylotype is observed in the heavy fractions from the 13C-vinyl chloride-amended cultures at both day 32 and day 45. Identifcation of degrading strains uses gene etnE, encoding for epoxyalkane coenzymeM-transferase, a critical enzyme in the pathway for vinyl chloride degradation |
| 4.4.1.34 | isoprene-epoxide-glutathione S-transferase |
degradation |
enzyme is involved in degradation of primary oxidation products of isoprene, cis-1,2-dichloroethanol, and trans-1,2-dichloroethanol |
| 4.5.1.3 | dichloromethane dehalogenase |
degradation |
enzyme activity in recombinant cells is 3 times higher than that in the wild-type Methylorubrum rhodesianum. Degradation efficiency of dichloromethane reaches 86.11% within 20 h and is highly associated with glutathione concentration |
| 5.2.1.4 | maleylpyruvate isomerase |
degradation |
the potential use of pure culture microbial cells for the cleanup of organophosphorus-pesticide-contaminated enviroments is highlighted, and the mechanisms for isocarbophos degradation are presented |
| 5.3.1.5 | xylose isomerase |
degradation |
enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan |
| 7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
degradation |
quantification of superoxide production from Escherichia coli complex I is very prone to artifacts |
| 7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
degradation |
strain Bacillus sp. SR-2-1/1 efficiently decolorizes azo dyes such as reactive black-5, reactive red-120, direct blue-1 and congo red through NADH-ubiquinone:oxidoreductase enzyme activity |
