EC Number   |
Recommended Name |
Application |
|---|
    3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
synthesis |
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide might influence substrate specificity by affecting the local structure of the CelK-specific N-terminal region containing an immunoglobulin-like domain |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
synthesis |
SCHEMA structure-guided recombination of fungal class II cellobiohydrolases (CBH II cellulases) from Humicola insolens, Hypocrea jecorina and Chaetomium thermophiulum and mathematical modeling yields a collection of highly thermostable CBH II chimeras with more activity than Humicola insolens CBH II after incubation at 63 °C. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyze phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyze as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and have pH/activity profiles as broad, or broader than, the parent enzymes. The best chimera with buildung blocks from all three organisms exhibits both relatively high specific activity and high thermostability |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
synthesis |
SCHEMA structure-guided recombination of fungal class II cellobiohydrolases (CBH II cellulases) from Humicola insolens, Hypocrea jecorina and Chaetomium thermophiulum and mathematical modeling yields a collection of highly thermostable CBH II chimeras. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyze phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyze as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and have pH/activity profiles as broad, or broader than, the parent enzymes. The best chimera with buildung blocks from all three organisms exhibits both relatively high specific activity and high thermostability |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
fluorescence-based assay for the transglycosylation activity of endo-beta-N-acetylglucosaminidases, highly sensitive, easy and quantitative method for screening endo-beta-N-acetylglucosaminidases with transglycosylation activity useful for glycoconjugate synthesis |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
highly efficient chemoenzymatic synthesis of N-glycopeptides. The use of the synthetic oligosaccharide oxazolines as the donor substrates for the transglycosylation expands the substrate availability and results in substantial enhancement of the synthetic efficiency |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
construction of natural or selectively modified glycopeptides by endoglycosidase-catalyzed transglycosylation |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
synthesis of oxazoline mono-, di-, tri- and hexasaccharides as potential glycosyl donors for enzyme catalyzed glycosylation of glycopeptides and glycoprotein remodelling |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
use of enzyme for synthesis of a human immunodeficiency virus type 1 glycopeptide with potent anti-HIV activity |
| 3.2.1.96 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase |
synthesis |
use of enzyme for the in vitro synthesis of glycoproteins containing complex type oligosaccharides from glycoproteins produced by yeast. Transglycosylation activity of enzyme can change high-mannose type oligosaccharides on glycoproteins to complex type ones |
| 3.2.1.97 | endo-alpha-N-acetylgalactosaminidase |
synthesis |
production of Galbeta(1-3)GalNAc from asialofetuin |
| 3.2.1.97 | endo-alpha-N-acetylgalactosaminidase |
synthesis |
synthesis of a wide variety of O-linked glycopeptides |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
synthesis |
very advantageous for obtaining pure maltohexaose |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
synthesis |
continuous production of maltohexaose on large scale using the immobilized exomaltohexaohydrolase |
| 3.2.1.98 | glucan 1,4-alpha-maltohexaosidase |
synthesis |
enzymatic reaction, transglycosylation, provides practical technique for industrial production of p-nitrophenyl alpha-maltoheptaoside, useful substrate for assay of human alpha-amylase in serum and urine |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
synthesis |
applied to the refinement of cotton fiber, enzyme is able to release the cotton fiber coating, yielding product of high quality but with lower amounts of wastes |
| 3.2.1.130 | glycoprotein endo-alpha-1,2-mannosidase |
synthesis |
the mutant has excellent transglycosylation activity and extremely low hydrolytic activity. The minimum motif required for glycosyl acceptor is Man-alpha-(1->2)Man. The synthetic utility of the enzyme is demonstrated by generation of a high-mannose-type undecasaccharide (Glc1Man9GlcNAc2) |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
synthesis |
application in enzymatic production of xylooligosaccharides from xylan. The high level of the thermostable alpha-glucuronidase from Thermotoga maritima, combined purification by a simple heat treament, has a considerable potential in the production of xylooligosaccharide, especially xylobiose |
| 3.2.1.132 | chitosanase |
synthesis |
valuable enzyme for the commercial production of chitosan oligosaccharides and other chitosan hydrolysates |
| 3.2.1.132 | chitosanase |
synthesis |
enhancement of enzyme production from 3.6 U/ml to 118 U/ml by substrate induction, statistical optimization of medium composition and culture conditions with colloidal chitosan being the best inducer and carbon source for chitosanase production |
| 3.2.1.132 | chitosanase |
synthesis |
enzyme is able to catalyze the synthesis of small amounts of chitooctaose from a mixture of chitobiose to chitoheptaose oligomers, possible through transglycosylation. Carrying out this process in reversed micellar microreactors formed by sodium bis-2(ethylhexyl) sulfosuccinate in isooctane significantly increases formation of high degree polymerized chitooligosaccharides. Pentamer and hexamer oligosaccharides are the main glycosyl acceptors |
| 3.2.1.132 | chitosanase |
synthesis |
expression in yeast cells as a whole-cell biocatalyst. Protein is localized to cell surface |
| 3.2.1.132 | chitosanase |
synthesis |
optimization of production conditions. In the optimized medium, strain JG produces 0.8 mmol per min and l of enzymic activity in 72 h |
| 3.2.1.132 | chitosanase |
synthesis |
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications |
| 3.2.1.132 | chitosanase |
synthesis |
the enzyme can be a competitive candidate for chitosan oligosaccharide-manufacturing industry |
| 3.2.1.132 | chitosanase |
synthesis |
the enzyme is a good candidate for production of beta-D-GlcN-(1->4)-beta-D-GlcN |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
thermostable maltogenic amylase with industrial potential, suitable for producing high maltose syrups from liquefied starch |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
industrial processes use heat-stable alpha-amylase for degrading starch |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
heterologous protein expression in Escherichia coli may contribute to better industrial production of maltogenic amylase |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
formation of maltosyl-tagatose from D-tagatose and maltotriose with maltogenic amylase. Glucosyl-tagatose is produced from maltosyl-tagatose by removal of a glucosyl moiety by glucoamylase. Glucosyl-tagatose has potential as a low-calorie sweetener and cryostabilizer |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
production of branched maltooligosaccharide |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
production of highly branched amylopectin and amylose from enzymatically modified rice starch |
| 3.2.1.133 | glucan 1,4-alpha-maltohydrolase |
synthesis |
the purified enzyme is employed to catalyze genistin glycosylation using gamma-cyclodextrin as both glucosyl donor and solubilizer |
| 3.2.1.135 | neopullulanase |
synthesis |
panose migth be used as an anticariogenic sweetener in foods, development of a system for continuous production of extremely high panose syrup from pullulan by employing the enzyme |
| 3.2.1.139 | alpha-glucuronidase |
synthesis |
hydrolysis of amylouronate to glucuronate by AUH-I |
| 3.2.1.140 | lacto-N-biosidase |
synthesis |
synthesis of Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc, i.e. lacto-neotetraose |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
production of trehalose from starch |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
production of trehalose from starch. Trehalose is utilized as a stabilizer for dried or frozen food, in cosmetics and in medicines as a drug additive |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
conditions for the production of trehalose from starch by thermostable maltooligosyl trehalose synthase and maltooligosyl trehalose trehalohydrolase from Sulfolubus acidocaldarius DSM 639 |
| 3.2.1.141 | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase |
synthesis |
trehalose production from starch |
| 3.2.1.142 | limit dextrinase |
synthesis |
expression of the limit dextrinase encoding gene fragment without signal peptide, with the Saccharomyces cerevisiae alpha-factor secretion signal under control of the alcohol oxidase 1 promoter, in Pichia pastoris leads to highly active barley limit dextrinase secreted during high cell-density fermentation. Optimization of a fedbatch fermentation procedure enables efficient production in a 5-l bioreactor, yielding 34 mg homogenous enzyme with 84% recovery |
| 3.2.1.151 | xyloglucan-specific endo-beta-1,4-glucanase |
synthesis |
mutant engineered xyloglucanases acting as glycosynthases are emerging as useful tools for the synthesis of large, complex polysaccharides, method development for robust and versatile method for the preparative synthesis of homogeneous xyloglucans with regular substitution patterns not available in nature, overview |
| 3.2.1.152 | mannosylglycoprotein endo-beta-mannosidase |
synthesis |
possible application in the synthesis of oligosaccharides containing mannosyl-beta-1,4-structures |
| 3.2.1.155 | xyloglucan-specific exo-beta-1,4-glucanase |
synthesis |
both the cane molasses medium and lactose-based conventional medium can serve as excellent growth media for Trichoderma reesei. The most abundant cellulolytic enzymes identified in both media are cellobiohydrolases (Cel7A/Cel6A) and endoglucanases (Cel7A/Cel5A) and are more abundant in CMM. Both media can serve as an inducer of xylanolytic enzymes. The main xylanases (XYNI/XYNIV) and xyloglucanase (Cel74A) are found at higher concentrations in the the cane molasses medium than lactose-based conventional medium |
| 3.2.1.157 | iota-carrageenase |
synthesis |
the enzyme can be utilized as a potential biocatalyst for producing iota-carrageenan oligosaccharides with different polymerization degrees |
| 3.2.1.163 | 1,6-alpha-D-mannosidase |
synthesis |
regioselective synthesis of mannobiose and mannotriose by reverse hydrolysis using the 1,6-alpha-D-mannosidase from Aspergillus phoenicis, method optimization, overview |
| 3.2.1.163 | 1,6-alpha-D-mannosidase |
synthesis |
synthesis of FimH receptor-active manno-oligosaccharides by reverse hydrolysis using alpha-mannosidases from Penicillium citrinum, Aspergillus phoenicis and almond in a sequential reaction process, method development and optimization, overview |
| 3.2.1.163 | 1,6-alpha-D-mannosidase |
synthesis |
the organism is employed in regioselective synthesis of manno-oligosaccharides involving the enzyme |
| 3.2.1.165 | exo-1,4-beta-D-glucosaminidase |
synthesis |
efficient tool for industrial production of glucosamine monosaccharide |
| 3.2.1.165 | exo-1,4-beta-D-glucosaminidase |
synthesis |
enzymatic formation of chitooligosaccharides by transglycosylation |
| 3.2.1.165 | exo-1,4-beta-D-glucosaminidase |
synthesis |
production of N-acetylglucosamine from chitosan by enzymatic degradation |
| 3.2.1.167 | baicalin-beta-D-glucuronidase |
synthesis |
synthesis of baicalein (i.e. 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one), a main active ingredient of Scutellaria sp. used in traditional Chinese medicine. It is difficult to obtain baicalein directly from skullaps because of its low content |
| 3.2.1.167 | baicalin-beta-D-glucuronidase |
synthesis |
the enzyme can be used for biotransformation of glycone baicalin to more pharmacologically active aglycone baicalein in extracts from Scutellaria baicalensis Georgi plant roots. Development of a chemically defined medium-based baicalein bioproduction process with a comparable yield compared to complex medium-based ones, overview |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
synthesis |
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
synthesis |
recombinant enzyme expressed in Zea mays is glycosylated and 6 kDa smaller than the native fungal protein. The cellobiohydrolase performs as well as or better than its fungal counterpart in releasing sugars from complex substrates such as pretreated corn stover or wood |
| 3.2.1.177 | alpha-D-xyloside xylohydrolase |
synthesis |
utility of enzyme AxlA from Aspergillus niger in supplementation of CTec2/HTec2 from Trichoderma reesei for enhancing release of free Glc and Xyl in combination with commercial enzyme cocktails from dicotyledonous and monocotyledonous plants, overview. AxlA supplementation also improves Glc yields from corn stover treated with the commercial cellulase Accellerase 1000 |
| 3.2.1.191 | ginsenosidase type III |
synthesis |
the beta-galactosidase from Aspergillus sp. can be useful for the mass production of rare ginsenosides |
| 3.2.1.191 | ginsenosidase type III |
synthesis |
the enzyme is applied for the production of gypenoside LXXV from gypenoside XVII at the gram-scale. The pure GypLXXV can be used for the study of anti-cancer effects against three kinds of cancer cells in vitro |
| 3.2.1.192 | ginsenoside Rb1 beta-glucosidase |
synthesis |
industrial applications of Lactobacillus rhamnosus strain GG to the biocatalysis of ginsenosides and/or other phytochemicals |
| 3.2.1.192 | ginsenoside Rb1 beta-glucosidase |
synthesis |
the beta-galactosidase from Aspergillus sp. can be useful for the mass production of rare ginsenosides |
| 3.2.1.192 | ginsenoside Rb1 beta-glucosidase |
synthesis |
the beta-glucosidase activity of Paenibacillus sp. MBT213 strain may be utilized in development of variety of health foods, dairy foods and pharmaceutical products |
| 3.2.1.193 | ginsenosidase type I |
synthesis |
in pharmaceutical and commercial industries, this recombinant Bgy2 can be suitable for producting ginsenoside Rd and compound K |
| 3.2.1.193 | ginsenosidase type I |
synthesis |
production of the pharmacologically active minor ginsenoside F2 from the major ginsenosides Rb1 and Rd by using the recombinant Lactococcus lactis strain expressing heterologous the beta-glucosidase gene |
| 3.2.1.194 | ginsenosidase type IV |
synthesis |
the enzyme is applied for the production of gypenoside LXXV from gypenoside XVII at the gram-scale. The pure GypLXXV can be used for the study of anti-cancer effects against three kinds of cancer cells in vitro |
| 3.2.1.195 | 20-O-multi-glycoside ginsenosidase |
synthesis |
in a reaction at 85°C and pH 5.0, 25 g/l of ginsenoside Rc is transformed into 21.8 g/l of ginsenoside Rd within 60 min, with a corresponding molar conversion of 99.4% and a high ginsenoside Rd productivity of 21800 mg/l/h |
| 3.2.1.206 | oleuropein beta-glucosidase |
synthesis |
high yield production of hydroxytyrosol from a commercially available oleuropein by using the immobilised recombinant EcSbgly from the hyperthermophilic archaeon Sulfolobus solfataricus on chitosan support |
| 3.2.1.211 | endo-(1->3)-fucoidanase |
synthesis |
the enzyme can be used for the manufacture of biologically active fucooligosaccharides from the fucoidans of Chorda filum |
| 3.2.1.211 | endo-(1->3)-fucoidanase |
synthesis |
the enzyme can be used for the manufacture of biologically active fucooligosaccharides from the fucoidans of Fucus evanescens |
| 3.2.1.212 | endo-(1->4)-fucoidanase |
synthesis |
the enzyme can be used for the modification of natural fucoidans to obtain more regular and easier characterized derivatives useful for research and practical applications |
| 3.2.2.4 | AMP nucleosidase |
synthesis |
stabilization of the adenylate energy charge |
| 3.2.2.4 | AMP nucleosidase |
synthesis |
purine nucleotide synthesis in procaryotes |
| 3.3.2.1 | isochorismatase |
synthesis |
synthesis of homochiral cis-cyclohexa-3,5-diene-1,2-diols |
| 3.3.2.8 | limonene-1,2-epoxide hydrolase |
synthesis |
application of directed evolution using iterative saturation mutagenesis as a means to engineer LEH mutants showing broad substrate scope with high stereoselectivity. Mutants are obtained which catalyze the desymmetrization of cyclopentene-oxide with stereoselective formation of either the (R,R)- or the (S,S)-diol on an optional basis. The mutants prove to be excellent catalysts for the desymmetrization of other meso-epoxides and for the hydrolytic kinetic resolution of racemic substrates |
| 3.3.2.9 | microsomal epoxide hydrolase |
synthesis |
the enantioselective enzyme is useful in production of chiral substances, e.g. production of (2R,3S)-ethyl 3-phenylglycidate with 95% enantiomeric excess and 26% yield in 12 h from 0.2% (w/v) of the racemat by whole cells of Pseudomonas sp. strain BZS21, maximal activity with dimethyl formamide as co-solvent |
| 3.3.2.9 | microsomal epoxide hydrolase |
synthesis |
the purified recombinant enzyme can be used as biocatalyst for kinetic resolution of racemic styrene oxide with the result of over 99% enantiopure (S)-styrene oxide in 23,5% yield |
| 3.3.2.9 | microsomal epoxide hydrolase |
synthesis |
enzyme prefers (R)-styrene oxide. Production of enantiopure (S)-styrene oxide by use of enzyme in batch kinetic resolution of racemic styrene oxide |
| 3.3.2.9 | microsomal epoxide hydrolase |
synthesis |
highly enantioselective synthesis of chiral 1,2 diols from epoxides in ionic liquid [bmim][PF6] or [bmim][Tf2N] in presence of 10% water |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
the enzyme may be a good biocatalyst for the preparation of enantiopure epoxides or diols |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
potential as biocatalyst for the preparation of enantiopure epoxides |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
the enantioselective enzyme is useful in production of chiral substances, e.g. production of (2R,3S)-ethyl 3-phenylglycidate with 95% enantiomeric excess and 26% yield in 12 h from 0.2% (w/v) of the racemat by whole cells of Pseudomonas sp. strain BZS21, maximal activity with dimethyl formamide as co-solvent |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
the enzyme is useful for enantioselective bio-organic synthesis of chiral substances |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
enantioselective hydrolysis of racemic styrene derivative via attack of the benzylic position results in formation of the correspponding (R)-diol with enantiomeric excess of up to 96% and more than 90% conversion |
| 3.3.2.10 | soluble epoxide hydrolase |
synthesis |
highly enantioselective synthesis of chiral 1,2 diols from epoxides in ionic liquid [bmim][PF6] or [bmim][Tf2N] in presence of 10% water |
| 3.4.11.1 | leucyl aminopeptidase |
synthesis |
production of polyketide antibiotics |
| 3.4.11.1 | leucyl aminopeptidase |
synthesis |
production of alpha-amino acids, which are intermediates in the synthesis of antibiotics, injectables, food and feed additives |
| 3.4.11.7 | glutamyl aminopeptidase |
synthesis |
the enzyme is interesting for an industrial application, because of the high specificity for N-terminal Asp and Glu |
| 3.4.11.10 | bacterial leucyl aminopeptidase |
synthesis |
LAP is an important enzyme for the industrial production of enantiomerically pure amino acids |
| 3.4.11.10 | bacterial leucyl aminopeptidase |
synthesis |
leucine aminopeptidase from Vibrio proteolyticus is a broad specificity N-terminal aminopeptidase that is widely used in pharmaceutical processes where the removal of N-terminal residues in recombinant proteins is required |
| 3.4.11.17 | tryptophanyl aminopeptidase |
synthesis |
part of method for Trp-production |
| 3.4.11.17 | tryptophanyl aminopeptidase |
synthesis |
the enzyme is useful for synthesis of L-Trp because it is not inhibited by high levels of the product |
| 3.4.11.18 | methionyl aminopeptidase |
synthesis |
recombinant human interferon alpha-2b is produced in Escherichia coli in two types of molecules, one type, in majority, having N-terminal methionine intact, whereas the other type, in minority, having the N-terminal methionine cleaved by methionine aminopeptidase of the host. The N-terminal methionine of the remaining molecules can be removed by utilizing methionine aminopeptidase from Pyrococcus furiosus |
| 3.4.11.18 | methionyl aminopeptidase |
synthesis |
the covalently immobilized enzyme bound to iminodiacetic acid-agarose or chloroacetamido-hexyl-agarose shows long-term stability and allows a continuous, heterogenous processing of N-terminal methionines, for example, in recombinant proteins. Activation by zinc avoids the introduction of heavy metals with toxicological liabilities and oxidative potential into biotechnological processes |
| 3.4.11.19 | D-stereospecific aminopeptidase |
synthesis |
production of D-amino acids from L-amino acid amides by combination of alpha-amino-epsilon-caprolactam racemase, EC 5.1.1.15, and enzyme. Yield of conversion of L-alanine amid is more than 99% |
| 3.4.11.19 | D-stereospecific aminopeptidase |
synthesis |
enantioselective hydrolysis of 2-aminobutanamide by 10 g/l recombinant cells harboring Dap results in 51.8% conversion in 10 min and 99.8% e.e, of (S)-2-aminobutanamide |
| 3.4.11.21 | aspartyl aminopeptidase |
synthesis |
dipeptide sweeteners aspartame and alitame |
| 3.4.11.23 | PepB aminopeptidase |
synthesis |
enzyme can be used for synthesis of alkoxy-serines from DL-beta-alkoxy-alpha-amino propionamides |
| 3.4.11.25 | beta-peptidyl aminopeptidase |
synthesis |
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo |
| 3.4.11.25 | beta-peptidyl aminopeptidase |
synthesis |
BapA catalyzes reversible protein acylation at the N-terminus. The selective modification can also be applied for protein labeling and tagging and should be generally useful, also to protect peptides and proteins from attack by common aminopeptidase |
| 3.4.13.20 | beta-Ala-His dipeptidase |
synthesis |
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo |
| 3.4.13.22 | D-Ala-D-Ala dipeptidase |
synthesis |
novel cell breakage method based on VanX. The D-Ala-D-Ala dipeptidase encoded in a vancomycin-resistant VanA gene cluster, exhibits a strong cell lysis activity when expressed in isolation in Escherichia coli. Coexpression of VanX with the target protein causes cell autolysis and release of the cellular content into the culture medium. Application of this strategy for two model proteins, a green fluorescent protein variant and Gaussia luciferase, and optimization of the autolysis conditions and coexpression vectors shows that the fluorescence activity of green fluorescent protein variant collected from the medium is identical to that of green fluorescent protein variant purified by conventional methods. Cell breakage by VanX-mediated autolysis is very simple to implement and will efficiently complement traditional methods |
| 3.4.13.22 | D-Ala-D-Ala dipeptidase |
synthesis |
strong bacteriolysis occurrs when isolated VanX is expressed in Escherichia coli at temperatures lower than 30°C. No cell lysis is observed when VanX is expressed, even in large quantities, in the cell inclusion bodies at 37°C, suggesting that a natively folded VanX is required for lysis. In addition, VanX mutants with suppressed dipeptidase activity do not lyse Escherichia coli cells, confirming that bacteriolysis originates from the dipeptidase activity of VanX. There are also shape changes in Escherichia coli cells undergoing VanX-mediated lysis, these changes may be classified into three classes: bursting, deformation, and leaking fluid |
