EC Number |
Recommended Name |
Application |
---|
6.3.5.2 | GMP synthase (glutamine-hydrolysing) |
synthesis |
industrial production of 5-guanylic acid |
6.3.5.2 | GMP synthase (glutamine-hydrolysing) |
synthesis |
importance of guanine synthesis in immune cell function, GMP synthetase is a potential target for immunosuppressive therapy |
6.3.5.11 | cobyrinate a,c-diamide synthase |
synthesis |
co-expression of the cobA gene from Propionibacterium freudenreichii and the cbiA, -C, -D, -E, -T, -F, -G, -H, -J, -K, -L, and -P genes from Salmonella enterica serovar typhimurium in Escherichia coli result in the production of cobyrinic acid a,c-diamide. Strains that have neither cbiP nor cbiA synthesized 1-desmethylcobyrinic acid even in the presence of cbiD, suggesting that CbiA and CbiP are necessary for CbiD activity |
6.4.1.1 | pyruvate carboxylase |
synthesis |
super-transfection of CHO cells with a mammalian construct bearing codon optimized yeast cytosolic pyruvate carboxylase PYC2 and a strong fusion promoter for optimal expression of PYC2 enzyme in order to control the lactate metabolism of mAb (IgG1-kappa) producing CHO clones. Presence of Pyc2 results in an improved mAb titer up to 5%, galactosylation up to 2.5folds, and mannosylation up to twofold |
6.4.1.1 | pyruvate carboxylase |
synthesis |
the presence of 10 mM L-aspartate in the production medium directly represses pyruvate carboxylase expression. This leads to limited malate flux which in turn regulates the malate/citrate antiporters resulting in increasing cis-aconitate decarboxylase activity to simultaneously convert cis-aconitate, citrate isomer, into itaconic acid |
6.4.1.2 | acetyl-CoA carboxylase |
synthesis |
expression in Bombyx mori using the silkworm NPV bacmid system. Recombinant protein shows biotinylation capacity,and exhibits posttranslational biotinylation and phosphorylation |
6.4.1.2 | acetyl-CoA carboxylase |
synthesis |
in yeast engineered to produce the polyketide 6-methylsalisylic acid (6-MSA), both 6-MSA and native fatty acid levels increase by 3fold in presence of mutant S1157A which is not deactivated when glucose is depleted |
6.4.1.3 | propionyl-CoA carboxylase |
synthesis |
expression of the propionyl-CoA carboxylase complex from Streptomyces coelicolor supports the highest levels of heterologous polyketide production in Escherichia coli. The molar yield of 6-deoxyerythronolide B of Escherichia coli, harboring the wild-type Streptomyces coelicolor propionyl-CoA carboxylase, is 1.2% |
6.5.1.1 | DNA ligase (ATP) |
synthesis |
plays an important role for recombination of DNA fragments in vitro |
6.5.1.2 | DNA ligase (NAD+) |
synthesis |
DNA ligase is an indispensible reagent in the chemical synthesis of double-stranded DNA of specific nucleotide sequence |
6.5.1.2 | DNA ligase (NAD+) |
synthesis |
an important use of DNA ligase is the preparation of recombinant DNA molecules for use in the cloning of DNA |
6.5.1.2 | DNA ligase (NAD+) |
synthesis |
DNA ligase is used for cDNA cloning by replacement synthesis |
6.5.1.3 | RNA ligase (ATP) |
synthesis |
synthesis of oligoribonucleotides with defined sequence |
6.5.1.3 | RNA ligase (ATP) |
synthesis |
RNA ligase-mediated method for the efficient creation of large, synthetic RNAs |
6.5.1.3 | RNA ligase (ATP) |
synthesis |
selective isotope labeling of RNA by introducing a labeled RNA segment via a two-step protocol, which uses T4 DNA ligase and T4 RNA ligase 1, and a one-pot protocol, which uses T4 RNA ligase 1 alone. Protection of termini is not required, provided segmentation sites can be chosen such that the segments fold into the target structure or target-like structures and thus are not trapped into stable alternate structures. Labeling protocols are generally applicable to large RNA molecules and can be extended to more than three segments |
6.5.1.3 | RNA ligase (ATP) |
synthesis |
efficient synthesis of 5' pre-adenylated DNA |
7.1.1.1 | proton-translocating NAD(P)+ transhydrogenase |
synthesis |
overexpression of pyridine nucleotide transhydrogenase, PntAB, results in a significant increase in biomass and glycolic acid titer and yield. Improved redox homeostasis resulting from PntAB overexpression positively affects the anabolic rate of the cell. PntAB overexpression result in 154 and 37% increase in NAD+/NADH ratio, at 48 and 72 h, respectively, while the the NADP+ concentrations are 70 and 30% lower at 24 and 72 h. Expression of PntAB in an optimized glycolic acid-producing strain improves the growth and product titer significantly |
7.1.1.3 | ubiquinol oxidase (H+-transporting) |
synthesis |
inactivating the cytochrome bd-II oxidase of the aerobic respiratory chain is a simple and effective strategy to improve poly(3-hydroxybutyrate) biosynthesis in Escherichia coli |
7.1.2.2 | H+-transporting two-sector ATPase |
synthesis |
concomitant increase in shoot Na+ accumulation and leaf succulence of plants, at optimal salinity increased CO2 assimilation, stomatal conductance, sub-stomatal CO2 concentration, transpiration rate, Rubisco specific activity and both high nitrogen-use efficiency and photosynthetic nitrogen-use efficiency, higher salt levels impair photosynthetic capacity via a stomatal limitation |
7.2.2.14 | P-type Mg2+ transporter |
synthesis |
by overexpression of mgtA in Escherichia coli, a concentration of 32.41 g succinic acid per liter with a yield of 0.81 g per g glucose, can be obtained in a batch fermentation by using the low-cost mixture of Mg(OH)2 and NH3-H2O to replace MgCO3 as the alkaline neutralizer. The effect of the inhibitory compounds in lignocellulosic hydrolyzates on cell growth and succinic acid production can be relieved. In a 3-liter bioreactor, the overall productivity and yield of succinic acid in the whole anaerobic stage are 2.15 g per liter and h and 0.86 g per g total sugar, respectively |
7.5.2.1 | ABC-type maltose transporter |
synthesis |
overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production, which is useful for the improvement of commercial antibiotic production using starch as the main carbon source in the fermentation process |