[go: up one dir, main page]

Isaya et al., 1988 - Google Patents

Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cells

Isaya et al., 1988

View PDF
Document ID
1519212499577178095
Author
Isaya G
Fenton W
Hendrick J
Furtak K
Kalousek F
Rosenberg L
Publication year
Publication venue
Molecular and cellular biology

External Links

Snippet

We have investigated mitochondrial import and processing of the precursor for human ornithine transcarbamylase (OTC; carbamoylphosphate: L-ornithine carbamoyltransferase, EC 2.1. 3.3) in HeLa cells stably transformed with cDNA sequences encoding OTC …
Continue reading at pmc.ncbi.nlm.nih.gov (PDF) (other versions)

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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • 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
    • 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
    • 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
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81—Protease inhibitors
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins

Similar Documents

Publication Publication Date Title
Maurizi et al. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.
JP2612874B2 (en) Methods of regulating protein metabolic stability
Abrahamson et al. Increased body temperature accelerates aggregation of the Leu-68--> Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy.
Mishkind et al. Functional determinants in transit sequences: import and partial maturation by vascular plant chloroplasts of the ribulose-1, 5-bisphosphate carboxylase small subunit of Chlamydomonas.
Guo et al. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity.
Isaya et al. Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide.
Dorner et al. The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins
CA2153254C (en) Cloning of enterokinase and method of use
Webster et al. The adenovirus protease is activated by a virus-coded disulphide-linked peptide
Pogliano et al. The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.
Skinner et al. Phospholipid transfer activity is relevant to but not sufficient for the essential function of the yeast SEC14 gene product.
West et al. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein.
Isaya et al. MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae
NO173741B (en) DNA SEQUENCE FOR MODIFIED PROTEIN C, VECTOR CONTAINING ITS, PATTERN CELLS TRANSFECTED WITH VECTORS, AND PROCEDURE FOR PREPARING THE PROTEIN
JP2688407B2 (en) Method for producing human protein C
US5712144A (en) Cloned factor C cDNA of the Singapore Horseshoe Crab, Carcinoscorpius rotundicauda and purification of Factor C proenzyme
Isaya et al. Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cells
Horwich et al. Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor.
Cocco et al. Inositides in the nucleus: presence and characterisation of the isozymes of phospholipase β family in NIH 3T3 cells
Pilgrim et al. Primary structure requirements for correct sorting of the yeast mitochondrial protein ADH III to the yeast mitochondrial matrix space
US6746859B1 (en) Cloning of enterokinase and method of use
JPH05504051A (en) Methods for endoproteolytic processing of (precursor) proteins
Behra et al. In vitro import into mitochondria of the precursor of mitochondrial aspartate aminotransferase.
Bowden et al. Abnormal fractionation of beta-lactamase in Escherichia coli: evidence for an interaction with the inner membrane in the absence of a leader peptide
Brennan et al. Specificity of yeast KEX2 protease for variant human proalbumins is identical to the in vivo specificity of the hepatic proalbumin convertase.