Kobes et al., 1971 - Google Patents
2-Keto-4-hydroxyglutarate aldolase of bovine liver. Schiff-base formation with 2-keto-4-hydroxyglutarate, pyruvate, and glyoxylateKobes et al., 1971
- Document ID
- 16626964816882972478
- Author
- Kobes R
- Dekker E
- Publication year
- Publication venue
- Biochemistry
External Links
Snippet
Rodger D. Kobesf and Eugene E. Dekker* abstract: 2-Keto-4-hydroxyglutarate aldolase, isolated in pure form (1300-fold purified) from bovine liver, binds any one of its substrates (2- keto-4-hydroxyglutarate, pyruvate, or glyoxylate) via an azomethine linkage. Using a …
- HHLFWLYXYJOTON-UHFFFAOYSA-M glyoxylate 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[O-]C(=O)C=O 0 title abstract description 63
Classifications
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Micro-organisms
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- 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)
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- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
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- 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
- C12P1/00—Preparation of compounds or compositions, not provided for in groups C12P3/00 - C12P39/00, by using micro-organisms or enzymes
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
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Gould et al. | Participation of Aminoacyl Transfer Ribonucleic Acid in Aminoacyl Phosphatidylglycerol Synthesis: II. Specificity of Alanyl Phosphatidylglycerol Synthetase | |
Frøyshov et al. | On the biosynthesis of bacitracin by a soluble enzyme complex from Bacillus licheniformis | |
Belendiuk et al. | CTP-phosphatidic acid cytidyltransferase from Saccharomyces cerevisiae. Partial purification, characterization, and kinetic behavior | |
Kubota et al. | Mechanism of inactivation of mammalian L-histidine decarboxylase by (S)-α-fluoromethylhistidine | |
Lange III et al. | Role of arginyl residues in directing carboxymethylation of horse liver alcohol dehydrogenase | |
Dekker et al. | Identification and cobamide coenzyme-dependent formation of 3, 5-diaminohexanoic acid, an intermediate in lysine fermentation | |
Wang et al. | Succinyl coenzyme A synthetase of Escherichia coli. Sequence of a peptide containing the active-site phosphohistidine residue | |
Akashi et al. | Biosynthesis of Enzyme-bound Formylvaline and Formylvalylglycine A Possible Initiation Complex for Gramicidin A Biosynthesis | |
Ushiroyama et al. | Amino acid sequence of histone H1 at the ADP‐ribose‐accepting site and ADP‐ribose· histone‐H1 adduct as an inhibitor of cyclic‐AMP‐dependent phosphorylation | |
Unger et al. | Action of a proline analogue, l-thiazolidine-4-carboxylic acid, in Escherichia coli | |
Palekar et al. | Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine | |
ALEXANDER | Studies on amino acid activating enzymes in thyroid glands | |
Akashi et al. | Enzyme-bound formylvaline and formylvalylglycine; an initiation complex for gramicidin A biosynthesis | |
Mishima et al. | DNA‐dependent mono (ADP‐ribosyl) ation of p33, an acceptor protein in hen liver nuclei |