Abstract:
It is intended to provide a process for producing a glycoprotein having a mammalian type sugar chain characterized by comprising transferring and expressing alpha-1,2-mannosidase in a sugar chain biosynthesis pathway gene mutant of a methylotroph yeast under the control by a potent promoter, culturing in a medium the methylotroph yeast cells having a foreign gene transferred thereinto, and then harvesting the glycoprotein having the mammalian type sugar chain from the culture medium. Using a newly bred methylotroph yeast carrying a sugar chain mutation, a neutral sugar chain identical with a high mannose type sugar chain produced by mammalian cells such as human cells or a glycoprotein having such a neutral sugar chain can be produced in a large amount at a high purity. By transferring a gene in a mammalian type sugar chain biosynthesis pathway into the above-described mutant, a mammalian type sugar chain such as a hybrid sugar chain or a complex sugar chain or a protein having a mammalian type sugar chain can be efficiently produced.
Abstract:
Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals.
Abstract:
This disclosure describes enzymes from the type II (a discrete set of enzymes) fatty acid synthesis ("FAS") pathway that can be used in combination with thiolases to operate a functional reversal of the β-oxidation cycle. A combination of thiolases with one or more of 3-oxoacyl-[acyl-carrier-protein] reductase (FabG, others), 3-hydroxyacyl-[acp] dehydratase (FabA, FabZ, others), and enoyl-[acyl-carrier-protein] reductase (FabI, FabK, FabL, FabV, others) yields a functional reversal of the β-oxidation cycle. If only one or two enzymes are used, the remaining enzymes will be traditional beta oxidation enzymes. Once this cycle is coupled with the appropriate priming and termination pathways, the production of carboxylic acids, alcohols, hydrocarbons, amines and their α-, β-, and ω-functionalized derivatives from renewable carbon sources can be achieved.
Abstract:
A mutant Pichia pastoris alcohol oxidase 1 (AOXl) promoter of the wild type Pichia pastoris AOXl promoter (SEQ ID No. 1) comprising at least one mutation selected from the group consisting of : a) a transcription factor binding site (TFBS) , b) nucleotides 170 to 235 (-784 to -719) , nucleotides 170 to 191 (-784 to -763) , nucleotides 192 to 213 (-762 to -741) , nucleotides 192 to 210 (-762 to -744) , nucleotides 207 to 209 (-747 to -745) , nucleotides 214 to 235 (-740 to -719) , nucleotides 304 to 350 (-650 to -604) , nucleotides 364 to 393 (-590 to -561) , nucleotides 434 to 508 (-520 to -446) , nucleotides 509 to 551 (-445 to -403) , nucleotides 552 to 560 (-402 to -394) , nucleotides 585 to 617 (-369 to -337) , nucleotides 621 to 660 (-333 to -294) , nucleotides 625 to 683 (-329 to -271) , nucleotides 736 to 741 (-218 to -213) , nucleotides 737 to 738 (-217 to -216) , nucleotides 726 to 755 (-228 to -199) , nucleotides 784 to 800 (-170 to -154) or nucleotides 823 to 861 (-131 to -93) of Seq ID No. 1, and combinations thereof .
Abstract translation:包含选自以下的至少一个突变的野生型巴斯德毕赤酵母AOX1启动子(SEQ ID No.1)的突变型巴斯德毕赤酵母醇氧化酶1(AOX1)启动子:a)转录因子结合位点(TFBS),b )核苷酸170至235(-784至-719),核苷酸170至191(-784至-763),核苷酸192至213(-762至-741),核苷酸192至210(-762至-744),核苷酸 207至209(-747至-745),核苷酸214至235(-740至-719),核苷酸304至350(-650至-604),核苷酸364至393(-590至-561),核苷酸434至 508(-520至-446),核苷酸509至551(-445至-403),核苷酸552至560(-402至-394),核苷酸585至617(-369至-337),核苷酸621至660( -333至-294),核苷酸625至683(-329至-271),核苷酸736至741(-218至-213),核苷酸737至738(-217至-216),核苷酸726至755(-228 至-199),核苷酸784至800(-170至-154)或核苷酸823至861(-131至-9 3)Seq ID No.1及其组合。
Abstract:
The invention relates to a method for combating disorders affecting the mitochondrial oxidative phosphorylation system by allotopic expression of the cyanide-insensitive alternative oxidase (AOX) in human cells. Successful expression of AOX in human cells and in Drosophila has been shown to confer spectacular cyanide-resistance to mitochondria, to alleviate oxidative stress, susceptibility to apoptosis and metabolic acidosis. AOX is well tolerated when expressed ubiquitously in a whole organism. AOX expression is a valuable tool to limit the deleterious consequences of respiratory chain deficiency.
Abstract:
The present invention relates to an edible composition, such as an oral care composition, a medicament, or a food and feed composition, comprising a sorbitol oxidase enzyme and sorbitol.