EC Number   |
Recommended Name |
Application |
|---|
   3.2.1.11 | dextranase |
degradation |
the hydrolysis of dextran under ultrasound/microwave irradiation shock treatment is significantly higher than those performed under ultrasound, microwave irradiation shock and conventional thermal incubation at all conditions studied. The maximum hydrolysis rate is observed when ultrasound/microwave irradiation shock (ultrasound of 50 W combined with microwave irradiation shock of 60 W at a sock rate of 20 s/min for 25 min) is used in which the dextran hydrolysis increases by 171.13% compared with routine conventional heating. Vmax and KM values of dextranase under ultrasound/microwave irradiation shock treatment are higher than those under ultrasound, microwave irradiation shock and conventional thermal incubation |
| 3.2.1.14 | chitinase |
degradation |
the enzyme is used for degradation of chitin-rich waste materials |
| 3.2.1.14 | chitinase |
degradation |
exo-acting enzyme with potential interest regarding the biodegradation of chitin waste or its bioconversion into biologically active products |
| 3.2.1.15 | endo-polygalacturonase |
degradation |
multiplicity of PGs that degrade the pectin component of the plant tissue in different fashions |
 3.2.1.21 | beta-glucosidase |
degradation |
beta-glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria |
| 3.2.1.21 | beta-glucosidase |
degradation |
a 3.43fold synergistic effect by combining with Trichoderma reesei cellulases is observed |
| 3.2.1.21 | beta-glucosidase |
degradation |
enzyme shows increased thermal stability and saccharification yield on pretreated corn stover compared with Hypocrea jecorina Cel3A |
| 3.2.1.21 | beta-glucosidase |
degradation |
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase |
| 3.2.1.21 | beta-glucosidase |
degradation |
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively |
| 3.2.1.21 | beta-glucosidase |
degradation |
addition of beta-glucosidase to the rice straw hydrolysis reaction containing a commercial cellulase results in increase of reducing sugars being released |
| 3.2.1.21 | beta-glucosidase |
degradation |
application of enzyme in fed-batch hydrolysis of cellulose and high-temperature simultaneous saccharification and fermentation. beta-Glucosidase is suitable for lignocellulose conversion into ethanol |
| 3.2.1.21 | beta-glucosidase |
degradation |
enzyme shows synergistic effects when commercial cellulase when is supplemented with the crude beta-glucosidase leading to improved sugar release of up to 548.4 mg/gds from paddy straw at 40°C |
| 3.2.1.21 | beta-glucosidase |
degradation |
highly efficient synergistic effects exist between TN0602 and cellulases for cellulose hydrolysis |
| 3.2.1.21 | beta-glucosidase |
degradation |
saccharification of pretreated paddy straw by supplementing beta-glucosidase enzyme results in 1.34fold higher glucose release |
| 3.2.1.21 | beta-glucosidase |
degradation |
the supplementation of BglP significantly enhances the glucose yield from sugarcane bagasse, especially in the presence of high concentrations of glucose or xylose |
| 3.2.1.21 | beta-glucosidase |
degradation |
use for bioethanol production from different cellulosic biomass sources. Using simultaneous saccharification and fermentation, 9.47 g/l and 14.32 g/l of bioethanol can be obtained from carboxymethyl cellulose and pretreated rice straw, respectively |
| 3.2.1.21 | beta-glucosidase |
degradation |
the high-catalytic turn-over rate by mutant enzyme D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures |
| 3.2.1.22 | alpha-galactosidase |
degradation |
enzyme completely hydrolyzes raffinose and stachyose present in soybeans and kidney beans at 50°C within 60 min |
| 3.2.1.23 | beta-galactosidase |
degradation |
evaluation of different commercial soluble beta-galactosidases for removal of the residual lactose in crude galactooligosaccharides. Best enzyme tested is lactase NL, with a hydrolytic activity of 286 IU/mg and a half-life of 9 h at 35°C in the presence of 1 mM Mn2+. The best reaction conditions are 35°C, 50% initial carbohydrate concentration and 135 IU/g, leading to 70% reduction of lactose in raw galactooligosaccharides, with an increase of 48% in monosaccharides and of 30% in galactooligosaccharides |
| 3.2.1.B28 | Pyrococcus furiosus beta-glycosidase |
degradation |
encapsulation of CelB into silica microcapsules for degradation of biomass. The encapsulated enzyme is active at 80-100°C, but diffusion of cellobiose into the silica microcapsules is a rate-limiting step |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
hydrolysis of water-soluble and water-insoluble arabinoxylan and whole vinasse by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei. The optimal dosages of the minimal enzyme cocktails are 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
in hydrolysis of corn stover hemicellulose, the xylose production increases by 94.9% and 140% when Trichoderma reesei hemicellulase is supplemented with purified beta-xylosidase and crude cell wall proteins of corn stover, respectively |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
enzyme increases reducing sugar release of birchwood xylan, beechwood xylan, and arabinoxylan by 6.4%, 13%, 15.8%, respectively, in synergistic action with endoxylanase. The late addition of the enzyme into reaction with endoxylanase results in a larger increase of reducing sugar release from pretreated barley straw that addition at the start or by treatment with endoxylanases alone. The increases observed are 6.3% and 13.8%, respectively |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
the enzyme has potential for promoting hemicellulose degradation and other industrial applications |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
degradation |
the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry |
| 3.2.1.40 | alpha-L-rhamnosidase |
degradation |
recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste |
| 3.2.1.41 | pullulanase |
degradation |
pullulanase is useful in the fermentation of high-gravity maize, together with other proteolytic and polysaccharide-degrading enzyme. Adding pullulanase resultes in the acceleration of the starch hydrolysis degree, which leads to lower amounts of unhydrolyzed dextrins and higher ethanol yield |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
enzyme of industrial interest because of its ability to improve hydrolytic action of other glycanases on hemicellulolytic polysaccharides |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
application potential for industrial purposes, biomass degradation and refining, extremely low end-product inhibition by arabinose further increases its applicability |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
enzymatic hydrolysis of wheat arabinoxylan. Treatment of water-soluble and water-insoluble wheat arabinoxylan with an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens (Abf II), the GH51 alpha-L-arabinofuranosidase from Meripilus giganteus (Abf III), a GH10 endo-1,4-beta-xylanase from Humicola insolens (Xyl III), and a GH3 beta-xylosidase from Trichoderma reesei releases 322 mg of arabinose and 512 mg of xylose per gram of water-soluble wheat arabinoxylan dry matter and 150 mg of arabinose and 266 mg of xylose per gram of water-insoluble wheat arabinoxylan dry matter after 24 h at pH 5, 50°C. A 10%:40%:50% mixture of Abf II, Abf III, and beta-xyl releases 56 mg of arabinose and 91 mg of xylose per gram of vinasse dry matter after 24 h at pH 5, 50°C. The optimal dosages of the enzyme cocktails are determined to be 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
enzyme shows synergistic effect on arabinose liberation from wheat arabinoxylan when combined with endoxylanase from Penicillium purpurogenum |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilized on commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
degradation |
the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan |
| 3.2.1.68 | isoamylase |
degradation |
thermophilic enzyme shows a potential to be used in industry to degrade the debranching points of starch at a high temperature |
| 3.2.1.73 | licheninase |
degradation |
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed |
| 3.2.1.73 | licheninase |
degradation |
the saccharification of untreated reed and rice straw powders by commercial enzymes (Celluclast 1.5 L and Novozym 188) is increased by 10.4 and 4.8%, respectively, by the addition of BGlc8H. In the presence of Ca2+ and BGlc8H, the saccharification of the pretreated reed and rice straw powders by the commercial enzymes is increased by 18.5 and 11.7%, respectively |
| 3.2.1.73 | licheninase |
degradation |
fermentation capacity of recombinant Bacillus subtilis expressing mutant K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P reaches 242.02 U ml/h. The addition of the mutant protein in Congress mashing significantly reduces the filtration time and viscosity of mash by 29.7% and 12.3%, respectively |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
degradation |
when assembled with the mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, a mixture of endoglucanase E and ManB at a molar ratio of 1:2 shows the highest synergistic effect of 2.4fold on locust bean gum degradation. The mixture at a ratio of 1:3 shows the highest synergistic effect of 2.8fold on guar gum |
| 3.2.1.78 | mannan endo-1,4-beta-mannosidase |
degradation |
the addition of Man26A as a supplement to the commercial enzyme mixture Celluclast 1.5 L and Novozyme 188 results in enhanced enzymatic hydrolysis of pretreated beechwood sawdust, the release of total reducing sugars and glucose is improved by 13 and 12%, respectively |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
degradation |
application of recombinant CBH II in hydrolysis of corn stover and rice straw pretreated with sodium hydroxide by improving the exo-exosynergism between CBH II and CBH I in Hypocrea jecorina. The yields 94.7% and 83.3% are achieved in the enzymatic hydrolysis of corn stover and rice straw pretreated by sodium hydroxide, respectively |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
degradation |
construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
degradation |
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
degradation |
combined use of isoforms CBH A and Cbh C on degradation of cotton. Conversion after 72 h is about 19 % by weight, with an almost fourfold increase in enzymatic hydrolysis yield by intermittent product removal of cellobiose with membrane filtration. A synergistic effect, achieving about 27 % substrate conversion, is obtained by addition of endo-1,4-beta-D-glucanase |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
degradation |
synergistic action of arase and pectinase can significantly improve the degradation of sugar beet pulp |
| 3.2.1.129 | endo-alpha-sialidase |
degradation |
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering (4.26 microgram enzyme + 39 mg hydrogel), in phosphate buffered saline (400 microl, pH 7.4), at 37°C, degradation speed 2-11 days depending on cross-linker amount (0.6, 0.8, 2 equivalents diepoxyoctane, no activity with 3 equivalents diepoxyoctane), hydrogel was coated with collagen I, poly-L-lysine/collagen I, or diluted matrigel for neurite formation in PC12 cells |
| 3.2.1.129 | endo-alpha-sialidase |
degradation |
degradation of non-toxic modified polysialic acid hydrogel scaffold in neuro-regenerative tissue engineering: no degradation in 12 days with 1 microg/ml active enzyme + 105 cubic mm hydrogel in phosphate buffered saline (pH 7.4), at room temperature, increase to 4 microg/ml at end of week 2 initiates degradation, total degradation after 4 weeks, hydrogel was coated with poly-L-lysine, poly-L-ornithine-laminin or collagen for neurite formation in neonatal and adult rat Schwann cells, neural rat stem cells, and dorsal root ganglionic cells from rats |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
degradation |
synergistic effects by use of enzyme and endoxylanase for degradation of oat xylan |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
degradation |
intracellular extract from Paenibacillus curdlanolyticus B-6, with synergistic alpha-glucuronidase and beta-xylosidase activities, degrades hexenuronosyl xylotriose to hexenuronic acid and xylotriose |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
degradation |
xylan degradation by endoxylanase Xyn10A is enhanced by about 10% in presence of AguA |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
degradation |
microcapsules from poly(vinyl alcohol) and hexamethylene diisocyanate, encapsulated with aqueous solution of maltogenic alpha-amylase from Bacillus stearothermophilus have potential application in biotechnology for saccharification of starch |
| 3.2.1.139 | alpha-glucuronidase |
degradation |
an enzymatic cocktail consisting of Agu115 with xylanase (Xyn10C), an alpha-L-arabinofuranosidase (AbfA), and a beta-xylosidase (XynB) achieves almost complete conversion of glucuronoarabinoxylan to arabinofuranose, xylopyranose, and methyl glucuronate monosaccharides. Addition of isoform Agu115 to the enzymatic cocktail contributes specifically to 25% of the conversion |
| 3.2.1.139 | alpha-glucuronidase |
degradation |
intracellular extract from Paenibacillus curdlanolyticus B-6, with synergistic alpha-glucuronidase and beta-xylosidase activities, degrades hexenuronosyl xylotriose to hexenuronic acid and xylotriose |
| 3.2.1.151 | xyloglucan-specific endo-beta-1,4-glucanase |
degradation |
xyloglucan endotransglucosylase can act as a cell wall-loosening enzyme |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
commercial cellulases contain mannan hydrolysing enzymes. Addition of 10 mg/ml mannan reduces the glucose yield of avicel (at 20 g/l) from 40.1 to 24.3%. The inhibitory effect is at least partly attributed to the inhibition of Cel7A(CBHI), but not on beta-glucosidase |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
comparison of the activity w ith Humicola jecorina Cel7A reveals a much higher hydrolytic rate for Humicola grisea Cel7A at both 65°C (4.8fold higher initial rate) and 38°C (3.3fold higher) |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
development of optimal enzyme mixtures of six Trichoderma reesei enzymes and five thermostable enzyme for the hydrolysis of hydrothermally pretreated wheat straw, alkaline oxidised sugar cane bagasse and steam-exploded bagasse by statistically designed experiments. The composition of optimal enzyme mixtures depends clearly on the substrate and on the enzyme system studied. The optimal enzyme mixture of thermostable enzymes is dominated by Cel7A and requires a relatively high amount of xylanase, whereas with Hypocrea jecorina enzymes, the high proportion of Cel7B appears to provide the required xylanase activity |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
enzyme works synergistically with the commercial enzyme cocktail Cellic R CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
degradation |
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities |
| 3.4.13.9 | Xaa-Pro dipeptidase |
degradation |
advantages of using Alteromonas recombinant prolidase in biodecontamination foams due to its high activity against G-type nerve agents, such as soman and sarin |
| 3.4.13.9 | Xaa-Pro dipeptidase |
degradation |
prolidase is able to degrade toxic organophosphorus compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman. Applications using prolidase to detoxify organophosphorous nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection |
| 3.4.17.18 | carboxypeptidase T |
degradation |
reconstruction of the primary specificity pocket of CpT to make it like CpB neither enhances the CpT5 activity with a substrate possessing C-terminal Arg, nor lowers the activity with a substrate carrying C-terminal Leu. Notwithstanding the considerable structural similarity of CpT and CpB, the mechanisms underlying their substrate specificities are different |
| 3.4.19.1 | acylaminoacyl-peptidase |
degradation |
AAP displays both exo- and endopeptidase activities |
| 3.4.19.12 | ubiquitinyl hydrolase 1 |
degradation |
a natural dodecapeptide amide from UCH-L3 with the sequence DPDELRFNAIAL is capable of binding to monoubiquitin and may enable the design of peptides with different affinities towards K48- and K63-linked polyubiquitin |
| 3.4.19.12 | ubiquitinyl hydrolase 1 |
degradation |
protein L-isoaspartate O-methyltransferase initiates the repair of isoaspartyl residues in aged or stress-damaged proteins in vivo, e.g. UCHL1 is a substrate for the L-isoaspartate methyltransferase in vivo |
| 3.4.21.7 | plasmin |
degradation |
cleavage at Arg336 is a central mechanism of plasmin-catalyzed factor VIII inactivation. Cleavages at Arg336 and Lys36 are selectively regulated by the A2 and A3-C1-C2 domains, respectively, interacting with plasmin |
| 3.4.21.61 | Kexin |
degradation |
ASP preferentially cleaves the peptide bond following two basic residues, one of which is Lys, but not the bond following a single basic residue. Tertiary structure around the catalytic domain of ASP resembles, but is not identical to that of furin |
| 3.4.21.61 | Kexin |
degradation |
Dpy-5 procollagen requires processing by BLI-4 for normal cuticle production |
| 3.4.21.61 | Kexin |
degradation |
PC1/3 is essential and sufficient for the production of the intestinal incretin hormone GIP |
| 3.4.21.62 | Subtilisin |
degradation |
subtilisin releases Phr signalling peptides derived from the C-terminus of their precursor proteins, but does not release Phr peptides derived from an internal portion of its precursor proteins |
| 3.4.21.64 | peptidase K |
degradation |
use of enzyme to degrade poly(L-lactide) film. Adsorption of enzyme to film is irreversible, enzyme moves on the surface of substrate to hydrolyze the film around it |
| 3.4.21.79 | granzyme B |
degradation |
human and murine GzmB are distinct enzymes with different substrate preferences. Subtle differences in enzyme structure can radically affect substrate selection. Caspases are essential for apoptosis initiated by mouse GzmB |
| 3.4.21.79 | granzyme B |
degradation |
human and murine GzmB are distinct enzymes with different substrate preferences. Subtle differences in enzyme structure can radically affect substrate selection. Caspases are not essential for apoptosis initiated by human GzmB |
| 3.4.21.112 | site-1 protease |
degradation |
S1P reduces the size of the luminal domain to prepare ATF6 to be an optimal S2P substrate |
| 3.4.24.B6 | matrix metalloproteinase-20 |
degradation |
MMP-20 processes dentin sialophosphoprotein into smaller subunits in the dentin matrix during odontogenesis |
| 3.4.24.12 | envelysin |
degradation |
one of the earliest zygotic genes activated, about 12-20 h after fertilization, the hatching enzyme is secreted, digesting the fertilization envelope and freeing the swimming blastula |
| 3.4.24.B16 | protease lasA |
degradation |
two-stage enzymatic reaction for the continuous measurement of LasA protease activity using a defined substrate, supplemented with Streptomyces griseus aminopeptidase for further cleavage of the product, rate of release of the chromophore can be measured spectrophotometrically |
| 3.4.24.B19 | i-AAA protease |
degradation |
essential function of the central pore loop for the ATP-dependent translocation of membrane proteins into a proteolytic cavity formed by AAA protease |
| 3.4.24.37 | saccharolysin |
degradation |
most likely major intracellular oligopeptidase responsible for the degradation of peptides resulting from nonvacuolar proteolysis |
| 3.4.24.37 | saccharolysin |
degradation |
Prd1 together with Mop112 is involved in the complete degradation of a large number of mitochondrial proteins to amino acids and therefore broadly influences the peptide efflux from mitochondria |
| 3.4.24.38 | gametolysin |
degradation |
degrades gametic cell walls, cell walls of vegetative cells and those of mother sporangial cells |
| 3.4.24.66 | choriolysin L |
degradation |
first choriolysin H swells the inner layer of egg envelope by limited digestion, and then choriolysin L solubilizes the swollen part of it completely |
| 3.4.24.67 | choriolysin H |
degradation |
HCE dissolves the inner layer of the egg envelope to facilitate hatching of the embryo |
| 3.4.24.77 | snapalysin |
degradation |
enzymatic and microbiological hydrolysis at the industrial level |
| 3.4.24.78 | gpr endopeptidase |
degradation |
D127 and D193 are essential for activity and autoprocessing |
| 3.4.24.82 | ADAMTS-4 endopeptidase |
degradation |
abrasion of cartilage aggrecan in rheumatoid arthritis and osteoarthritis |
| 3.4.24.82 | ADAMTS-4 endopeptidase |
degradation |
degradation of cartilage in late-stage Lyme arthritis |
| 3.4.24.82 | ADAMTS-4 endopeptidase |
degradation |
degradation of cartilage proteoglycan (aggrecan) in osteoarthritis and rheumatoid arthritis |
| 3.4.25.1 | proteasome endopeptidase complex |
degradation |
targeted proteasomal knockdown of GFP is induced by use of a specific anti-GFP nanobody in plants. GFP is depleted by a chimeric nanobody fused to a distinct F-box domain, which enables protein degradation via the ubiquitin proteasome pathway |
| 3.5.1.9 | arylformamidase |
degradation |
aerobic degradation of L-tryptophan |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
degradation |
biotic interaction between earthworms and the bacterial community involved in degradation of the herbicide atrazine in a maize-cropped soil, earthworms significantly affect the structure of the soil bacterial communities in the biostructures, they reduce the size of the population of Pseudomonas sp. ADP, thereby contributing to the diminution of the atrazine-degrading genetic potential in soil microsites |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
degradation |
broad level bacterial community interactions that are involved in atrazine degradation in nature |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
degradation |
broad level bacterial community interactions that are involved in atrazine degradation in nature, Nocardia sp. plays a crucial role for stable maintenance of the degrader community, dechlorination of atrazine is carried out exclusively by Nocardia sp. which apart from the atzC gene contains the trzN gene |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
degradation |
enzyme degrades the herbicide atrazine, biodegredation in the microcosm appears to occur predominantely by Nocardioides sp. to yield cyanuric acid, which can be mineralised by other relatively ubiquitous microbes |
| 3.5.4.42 | N-isopropylammelide isopropylaminohydrolase |
degradation |
novel atrazine catabolic pathway combining trzN with atzB and atzC, the gene products dechlorinate and then dealkylate atrazine |
