EC Number   |
Recommended Name |
Application |
|---|
    5.3.1.8 | mannose-6-phosphate isomerase |
biotechnology |
use of enzyme as selectable marker for transformation of Oriza sativa immature embryo via Agrobacterium |
| 5.3.1.8 | mannose-6-phosphate isomerase |
biotechnology |
use of enzyme gene as selectable marker for transformation of Penniseum glaucum. Enzyme gene is a superior selectable marker for improving transformation efficiencies when compared to antibiotic or herbicide selectable marker genes |
| 5.3.1.8 | mannose-6-phosphate isomerase |
biotechnology |
the pmi/mannose selection system is highly efficient for producing transgenic Oncidium Gower Ramsey without using antibiotics or herbicides |
| 5.3.1.24 | phosphoribosylanthranilate isomerase |
biotechnology |
the work provides a method of exchanging variably sized loops within the (beta/alpha)8 fold, affording a novel starting point for the screening of novel activities as well as modest diversions from an original activity |
| 5.3.3.2 | isopentenyl-diphosphate DELTA-isomerase |
biotechnology |
an Escherichia coli strain is engineered for isoprenoid ether lipid biosynthesis through digeranylgeranylglycerylphosphate, DGGGP |
| 5.3.3.2 | isopentenyl-diphosphate DELTA-isomerase |
biotechnology |
overexpression of SlIPI in engineered Escherichia coli can promote the biosynthesis of beta-carotene in bacteria, the result provides a foundation for terpenoid metabolic engineering using the SlIPI gene |
| 5.3.3.2 | isopentenyl-diphosphate DELTA-isomerase |
biotechnology |
the prenyl alcohol production by Escherichia coli transformants with overexpression of isoprenoid biosynthesis genes is examined |
| 5.3.3.B2 | linoleate (10E,12Z)-isomerase |
biotechnology |
the enzyme shows the ability to produce fatty acid components of vegetable oils with novel physiological activities in crops |
| 5.3.4.1 | protein disulfide-isomerase |
biotechnology |
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhance by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 3fold, production method evaluation |
| 5.3.4.1 | protein disulfide-isomerase |
biotechnology |
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhanced by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 clone 3fold, production method evaluation |
| 5.3.99.6 | allene-oxide cyclase |
biotechnology |
constitutive overexpression of enzyme, 53fold increase of 12-oxo-phytodienoic acid methyl ester in stamen, 51fold increase of jasmonic acid in buds and 7.5fold increase in sepals. Increase in jasmonates and octadecanoids is accompanied by decreased levels of free lipid hydro(per)oxy compounds |
| 5.4.2.7 | phosphopentomutase |
biotechnology |
the Escherichia coli expressing Bacillus sphaericus phosphopentomutase is an excellent catalyst as to production of 2'-deoxyribonucleoside in the presence of acetaldehyde and phosphorylated compounds |
| 5.4.2.8 | phosphomannomutase |
biotechnology |
enzymatic synthesis of TMP and 2-deoxy-6-phosphate glucose can successfully produce large amount of TDP-2-deoxy-glucose in one-pot by employing phosphomannomutase |
| 5.4.2.8 | phosphomannomutase |
biotechnology |
the double mutant lacking the PMI and PMM genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins, with further genetic engineering these mutants may activate alternative hexoses as GDP-sugars for transfer to aglycones in vivo |
| 5.5.1.4 | inositol-3-phosphate synthase |
biotechnology |
the enzyme is a possible target for genetic modification of maize plants to get low phytic acid containing variants |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
incorporation of unusual specific amino acids into proteins in in vitro translation systems by mutant enzyme with altered substrate specificity. e.g. mutant Y32Q/D158A |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
site-specific incorporation of 3-iodo-L-tyrosine into proteins in a cell-free system for use in specialized in vitro translation systems |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
use of mutant Y43G for specialized protein synthesis as a carrier for additional amino acids and derivatives for use in e.g. crystal structure determination by X-ray diffraction |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
a mutant Methanococcus jannaschii tyrosyl amber suppressor tRNA, Tyr MjtRNA CUR/tyrosyl-tRNA synthetase (MjTyrRS) pair is developed to uniquely incorporate phenylselenocysteine in response to the amber TAG codon in Escherichia coli. After being efficiently converted into dehydroalanine under mild conditions, Michael addition reactions with the corresponding thiols can be used to synthesize N-methyl- and N-acetyl-lysine analogues |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
Escherichia coli-based cell-free system for the production of proteins with a non-natural amino acid incorporated site-specifically is described. A mutant Methanococcus jannaschii tyrosyl-tRNA synthetase (mTyrRS) and tRNATyr pair are used as orthogonal elements. The mTyrRS experienced proteolysis and modified protein yields improves with higher synthetase addition (200-300 mg/mL) |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
a rapid, straightforward, one plasmid dual positive/negative selection system for the evolution of aminoacyl-tRNA synthetases with altered specifities in Escherichia coli is developed |
| 6.1.1.1 | tyrosine-tRNA ligase |
biotechnology |
the present engineering allows Escherichia coli TyrRS variants for non-natural amino acids to be developed in Escherichia coli, for use in both eukaryotic and bacterial cells for genetic code expansion |
| 6.1.1.2 | tryptophan-tRNA ligase |
biotechnology |
EcTrpRS is used as a model system for in silicio docking studies with various Trp analogs using the FlexX-Pharm strategy. Relative binding energies for Trp analogs in TrpRS are calculated that correlate well with their translational activities in Escherichia coli. FlexX-Pharm predicted the binding sites of fluoro-, amino-, hydroxyl- and aza-containing Trp analogs within 1.5 A of Trp in the homology model of EcTrpRS |
| 6.1.1.20 | phenylalanine-tRNA ligase |
biotechnology |
design of an enzyme variant which incorporates aryl ketones into proteins |
| 6.1.1.20 | phenylalanine-tRNA ligase |
biotechnology |
misacylation of suppressor tRNAPhe CUA by the PheRS mutant A294G with 4-iodo-L-phenylalanine might be useful in application in protein engineering since an aryl iodide tag on proteins can be used for site-specific functionalization of proteins, used for cell-free protein synthesis as a stoichiometric reagent, overview |
| 6.1.1.27 | O-phospho-L-serine-tRNA ligase |
biotechnology |
the mutant SepRS-tRNA pairs may be useful for translational incorporation of O-phosphoserine into proteins in response to the stop codons UGA and UAG, so that it could ligate O-phosphoserine to a suppressor tRNA for genetic-code expansion |
| 6.2.1.12 | 4-coumarate-CoA ligase |
biotechnology |
viability of a flavonoid network to utilize acrylic acid analogues and describe the combinatorial mutasynthesis of novel unnatural flavonoids using recombinant Saccharomyces cerevisiae, overview |
| 6.3.1.20 | lipoate-protein ligase |
biotechnology |
the enzyme lipoic acid ligase (LplA) can be used for PRIME (probe incorporation mediated by enzymes) labeling, a rapid and specific fluorescent labeling method of the protein of interest by LplA |
| 6.3.2.2 | glutamate-cysteine ligase |
biotechnology |
a protein transduction approach whereby recombinant GCL protein can be rapidly and directly transferred into cells when coupled to the HIV TAT protein transduction domain. The TAT-GCL fusion proteins are capable of heterodimerization and formation of functional GCL holoenzyme in vitro. Exposure of Hepa-1c1c7 cells to the TAT-GCL fusion proteins results in the time- and dose-dependent transduction of both GCL subunits and increased cellular GCL activity and glutathione levels. A heterodimerization-competent, enzymatically deficient GCLC-TAT mutant was also generated in an attempt to create a dominant-negative suppressor of GCL |
| 6.3.2.3 | glutathione synthase |
biotechnology |
overexpression of the enzyme in transgenic plants offers a promising strategy for the production of plants with superior heavy-metal phytoremediation capacity |
| 6.3.2.12 | dihydrofolate synthase |
biotechnology |
production of active dihidrofolate synthase in milligram scale |
| 6.3.2.26 | N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase |
biotechnology |
production of beta-lactam antibiotics |
| 6.3.4.16 | carbamoyl-phosphate synthase (ammonia) |
biotechnology |
ammonia elimination as functional marker in hepatocyte cultivation and zonation in a bioreactor, and construction of a bioartificial liver, overview |
| 6.3.5.6 | asparaginyl-tRNA synthase (glutamine-hydrolysing) |
biotechnology |
inhibitor represents a lead scaffold to discover and develop antifilarial drugs |
| 6.4.1.1 | pyruvate carboxylase |
biotechnology |
coexpression of recombinant pyruvate coarboxylase in BHK-21 cells improves the production of human erythropoietin in a continuously perfused bioreactor |
| 6.4.1.1 | pyruvate carboxylase |
biotechnology |
FLAG-tagged human pyruvate carboxylase is introduced into a dihydrofolate-deficient CHO cell line DG44. Through the expression of the human pyruvate carboxylase enzyme, lactate formation in CHO cell culture can be efficiently reduced. This effect of expression of the human pyruvate carboxylase is observed not only in adherent batch culture using the serum-containing medium but in the serum-free suspension fed-batch culture as well, demonstrating its potential use to extend the culture longevity of CHO cell culture, which often shows a significant accumulation of lactate |
| 6.4.1.2 | acetyl-CoA carboxylase |
biotechnology |
the enzyme is a target for development of herbicides |
| 6.5.1.2 | DNA ligase (NAD+) |
biotechnology |
LigN is unique amongst DNA ligase enzymes in displaying maximal DNA strand joining activity at above 3 M salt levels. As such the LigN enzyme has potential both as a novel tool for biotechnology and as a model enzyme for studying the adaptation of proteins to high intracellular salt levels |
| 7.2.2.3 | P-type Na+ transporter |
biotechnology |
expression of triple hemagglutinin-tagged enzyme in Nicotiana tabacum confers increased NaCl and LiCl tolerance to cells. Under moderate slat stress, enzyme expression results in accumulation of less Na+, Li+ and K+ than in wild-type |
| 7.2.2.10 | P-type Ca2+ transporter |
biotechnology |
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals |
| 7.2.2.14 | P-type Mg2+ transporter |
biotechnology |
Overexpression of enzyme in Escherichia coli results in formation of inclusion bodies. Co-expression of DnaK/DnaJ prevents inclusion bodies and leads to the integration of more enzyme into the membrane. Co-expression of GroEL/GroES, Ffh/4.5S-RNA or SecA are less effective |
| 7.2.2.21 | Cd2+-exporting ATPase |
biotechnology |
expression of enzyme in Saccharomyces cerevisiae strikingly decreases Cd2+ tolerance of yeast cells. Yeast expressing the non-functional mutant D398A can grow on selective medium containing up to 0.1 mM Cd2+, while those expressing the intact enzyme cannot grow in presence of 0.001 mM Cd2+. Enzyme is localized in the endoplasmic reticulum, so hypersensitivity to Cd2+ is due to Cd2+ accumulation in the reticulum lumen. Zn2+ does not protect cells against Cd2+ poisoning |
| 7.2.2.22 | P-type Mn2+ transporter |
biotechnology |
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals |
| 7.4.2.8 | protein-secreting ATPase |
biotechnology |
glutathione S-transferase-enzyme fusion protein functions analogously to native protein. Overexpression of regulatory protein YscL impairs secretion |
