Lee et al., 1998 - Google Patents
Cloning and expression of cDNA for a human Siaα2, 3Galβ1, 4GlcNA: α2, 8-sialyltransferase (hST8Sia III)Lee et al., 1998
- Document ID
- 18054505656127415971
- Author
- Lee Y
- Kim Y
- Lee K
- Kim K
- Kim B
- Kim H
- Kim C
- Do S
- Publication year
- Publication venue
- Archives of biochemistry and biophysics
External Links
Snippet
The cDNA encoding human Sia-α2, 3-Gal-β1, 4-GlcNAc-R: α2, 8-sialyltransferase, hST8Sia III, was isolated by screening of a human brain cDNA library with polymerase chain reaction- amplified DNA probe generated from the sequence of mouse ST8Sia III (mST8Sia III) and by …
- 229920002676 Complementary DNA 0 title abstract description 33
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8243—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine
- C12N15/8245—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine involving modified carbohydrate or sugar alcohol metabolism, e.g. starch biosynthesis
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/1029—Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y204/00—Glycosyltransferases (2.4)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y206/00—Transferases transferring nitrogenous groups (2.6)
- C12Y206/01—Transaminases (2.6.1)
- C12Y206/01005—Tyrosine transaminase (2.6.1.5)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Henion et al. | Defining the minimal size of catalytically active primate α1, 3 galactosyltransferase: structure-function studies on the recombinant truncated enzyme | |
JPH09501317A (en) | Compositions and methods for producing sialyltransferases | |
Kitagawa et al. | Cloning of a novel alpha 2, 3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. | |
Wen et al. | Primary structure of Gal beta 1, 3 (4) GlcNAc alpha 2, 3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family. | |
LEE et al. | Molecular cloning and expression of Galβ1, 3GalNAcα2, 3‐sialyltransferase from mouse brain | |
Kumar et al. | Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation. | |
US7709234B2 (en) | α-1,3-fucosyltransferase | |
Lee et al. | Cloning and expression of cDNA for a human Siaα2, 3Galβ1, 4GlcNA: α2, 8-sialyltransferase (hST8Sia III) | |
Montiel et al. | Molecular cloning, gene organization and expression of the human UDP-GalNAc: Neu5Acalpha2-3Galbeta-R beta1, 4-N-acetylgalactosaminyltransferase responsible for the biosynthesis of the blood group Sda/Cad antigen: evidence for an unusual extended cytoplasmic domain | |
Krzewinski‐Recchi et al. | Identification and functional expression of a second human β‐galactoside α2, 6‐sialyltransferase, ST6Gal II | |
Kim et al. | Molecular cloning and expression of human α2, 8-sialyltransferase (hST8Sia V) | |
AU668714B2 (en) | Compositions and methods for the identification and synthesis of sialyltransferases | |
Harduin-Lepers et al. | Cloning, expression and gene organization of a human Neu5Acα2–3Galβ1–3GalNAc α2, 6-sialyltransferase: hST6GalNAc IV | |
Kurosawa et al. | Molecular cloning and expression of chick embryo Galβ1, 4GlcNAcα2, 6‐sialyltransferase: Comparison with the mammalian enzyme | |
JP2810635B2 (en) | New sugar chain synthase | |
AU662441B2 (en) | N-acetylglucosaminyltransferase V coding sequences | |
US7670815B2 (en) | N-acetylglucosaminyltransferase Vb coding sequences, recombinant cells and methods | |
EP1295946B1 (en) | Sulfate transferase and dna encoding this enzyme | |
Meurer et al. | cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase | |
Sotiropoulou et al. | Identification and functional characterization of a human GalNAc α 2, 6-sialyltransferase with altered expression in breast cancer | |
Lee et al. | Molecular cloning and functional expression of two members of mouse NeuAc� 2, 3Gal� 1, 3GalNAc GalNAc� 2, 6-sialyltransferase family, ST6GalNAc III and IV | |
Mucha et al. | Two closely related forms of UDP-GlcNAc: α6-D-mannoside β1, 2-N-acetylglucosaminyltransferase II occur in the clawed frog Xenopus laevis | |
Kim et al. | Molecular cloning and sequence analysis of human GM3 synthase (hST3Gal V) | |
VALLEJO-RUIZ et al. | Cloning, expression and gene organization of a human Neu5Acα2–3Galβ1–3GalNAc α2, 6-sialyltransferase: hST6GalNAc IV1 | |
Lee et al. | Molecular Cloning and Substrate Specificity of Human NeuAc ${\alpha} $2, 3Gal ${\beta} $1, 3GalNAc GalNac ${\alpha} $2, 6-Sialyltransferase (hST6GalNac IV) |