Results 1 to 10 of about 196,977 (320)

Efficient <i>trans</i>-aconitic acid production using systematically metabolic engineered <i>Escherichia coli</i>. [PDF]

Synth Syst Biotechnol
Guo L, Cheng Y, Tan X, Zhang H, Yu H, Tian W, Liu M, Sun W, Gao K, Jiang T, Kang Q, Meng W, Liu Y, Kang Z, Lü C, Gao C, Xu P, Ma C.   +17 more
europepmc   +1 more source

Resurrection and characterization of ancestral xylose transporters enhance the capability of xylose uptake in the mixed sugar co-fermentation of Recombinant Saccharomyces cerevisiae. [PDF]

Bioresour Bioprocess
Zhang P, He Z, Li H, Jiang Z.
europepmc   +1 more source

Dual-Enzyme Co-Catalysis Strategy for Fructooligosaccharides (FOS) Biocatalytic Synthesis for Valorization of Low-Cost Byproduct Sugarcane Molasses. [PDF]

Foods
Chen GL, Chen J, Dai JX, Dai XH, Zheng FJ, Verma KK, Yang LF.   +6 more
europepmc   +1 more source

Protein losing enteropathy due to congenital disorder of glycosylation: A case report. [PDF]

SAGE Open Med Case Rep
Odenthal J, Lin HC, Trieschmann K.
europepmc   +1 more source

Protein disulfide isomerase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
Bonney, Wilkinson, Hiram F, Gilbert
openaire   +2 more sources

Cloning and overexpression of rhamnose isomerase and fucose isomerase

Bioorganic & Medicinal Chemistry, 1995
Rhamnose isomerase and fucose isomerase were overexpressed in E. coli, purified and characterized. The rhamnose isomerase gene was ligated to the restriction sites of PstI and Hind III of vector pTrcHis and the fucose isomerase gene was ligated to the EcoRI and PstI sites of vector pKK223-3 for overexpression of the enzymes in E.
E, Garcia-Junceda, G J, Shen, R, Alajarin, C H, Wong   +3 more
openaire   +2 more sources

Prolyl isomerases in yeast

Frontiers in Bioscience, 2004
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1).
Miguel, Arevalo-Rodriguez, Xiaoyun, Wu, Steven D, Hanes, Joseph, Heitman   +3 more
openaire   +2 more sources