alpha-ketobutyric acid and alpha-ketoisovalerate

alpha-ketobutyric acid has been researched along with alpha-ketoisovalerate in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (11.11)18.2507
2000's5 (55.56)29.6817
2010's3 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Halestrap, AP; Manning Fox, JE; Meredith, D1
Gold, M; Jones, JB; Kallwass, HK; Kay, CM; Parris, W; Sakowicz, R1
Gelev, VM; Gross, JD; Wagner, G1
Binder, S; Schuster, J1
Eggeling, L; Kennerknecht, N; Marienhagen, J; Sahm, H1
Auer, R; Hommel, U; Kloiber, K; Konrat, R; Kontaxis, G; Ledolter, K; Lichtenecker, R; Ruedisser, S; Schedlbauer, A; Schmid, W; Tollinger, M1
Brigham, CJ; Lu, J; Plassmeier, JK; Sinskey, AJ1
Glaser, RW; Hunt, JF; Jouhten, P; Maaheimo, H; Montelione, GT; Swapna, GVT; Szyperski, T; Xu, Y; Yu, XW; Zhang, M1
Lee, HS; Park, J; Yeon, YJ; Yoo, YJ1

Other Studies

9 other study(ies) available for alpha-ketobutyric acid and alpha-ketoisovalerate

ArticleYear
Characterisation of human monocarboxylate transporter 4 substantiates its role in lactic acid efflux from skeletal muscle.
    The Journal of physiology, 2000, Dec-01, Volume: 529 Pt 2

    Topics: Animals; Biological Transport, Active; Carrier Proteins; Cells, Cultured; Fluoresceins; Fluorescent Dyes; Humans; Kinetics; Lactic Acid; Monocarboxylic Acid Transporters; Muscle Proteins; Muscle, Skeletal; Oocytes; Protein Isoforms; Substrate Specificity; Xenopus

2000
Threonine 246 at the active site of the L-lactate dehydrogenase of Bacillus stearothermophilus is important for catalysis but not for substrate binding.
    Biochemistry, 1993, Nov-30, Volume: 32, Issue:47

    Topics: Base Sequence; Butyrates; Catalysis; Circular Dichroism; Geobacillus stearothermophilus; Hemiterpenes; Keto Acids; L-Lactate Dehydrogenase; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylpyruvic Acids; Pyruvates; Substrate Specificity; Threonine

1993
A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes.
    Journal of biomolecular NMR, 2003, Volume: 25, Issue:3

    Topics: Butyrates; Cholic Acids; Eukaryotic Initiation Factor-4E; Hemiterpenes; Isotopes; Keto Acids; Ligands; Magnetic Resonance Spectroscopy; Micelles; Models, Chemical; Oxalates; Proteins; Saccharomyces cerevisiae; Sensitivity and Specificity; Statistics as Topic

2003
The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana.
    Plant molecular biology, 2005, Volume: 57, Issue:2

    Topics: Amino Acids, Branched-Chain; Aminobutyrates; Arabidopsis; Arabidopsis Proteins; Butyrates; Deamination; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Glucuronidase; Hemiterpenes; Isoleucine; Keto Acids; Kinetics; Leucine; Methionine; Mitochondrial Proteins; Plants, Genetically Modified; Promoter Regions, Genetic; Recombinant Fusion Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Seedlings; Substrate Specificity; Transaminases; Transcription, Genetic; Valine

2005
Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum.
    Journal of bacteriology, 2005, Volume: 187, Issue:22

    Topics: Alanine; Aspartic Acid; Bacterial Proteins; Butyrates; Carbon-Sulfur Lyases; Corynebacterium glutamicum; Gene Deletion; Glutamic Acid; Hemiterpenes; Keto Acids; Phenylpyruvic Acids; Pyruvic Acid; Substrate Specificity; Transaminases

2005
Direct methods and residue type specific isotope labeling in NMR structure determination and model-driven sequential assignment.
    Journal of biomolecular NMR, 2008, Volume: 42, Issue:2

    Topics: Butyrates; Hemiterpenes; Isotope Labeling; Keto Acids; Models, Molecular; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Proteins

2008
Characterization and modification of enzymes in the 2-ketoisovalerate biosynthesis pathway of Ralstonia eutropha H16.
    Applied microbiology and biotechnology, 2015, Volume: 99, Issue:2

    Topics: Acetolactate Synthase; Bacterial Proteins; Biosynthetic Pathways; Butyrates; Culture Media; Cupriavidus necator; DNA, Bacterial; Hemiterpenes; Hydro-Lyases; Isoleucine; Keto Acids; Ketol-Acid Reductoisomerase; Leucine; Mutagenesis, Site-Directed; Valine

2015
    The FEBS journal, 2017, Volume: 284, Issue:18

    Topics: Aerobiosis; Batch Cell Culture Techniques; Butyrates; Carbon Isotopes; Citric Acid Cycle; Glucose; Hemiterpenes; Isoleucine; Keto Acids; Leucine; Magnetic Resonance Spectroscopy; Metabolome; Mitochondria; Pentose Phosphate Pathway; Pichia; Pyruvic Acid; Saccharomyces cerevisiae; Valine

2017
Engineering D-Lactate Dehydrogenase from Pediococcus acidilactici for Improved Activity on 2-Hydroxy Acids with Bulky C
    Applied biochemistry and biotechnology, 2019, Volume: 189, Issue:4

    Topics: Amino Acid Substitution; Bacterial Proteins; Biocatalysis; Butyrates; Hemiterpenes; Keto Acids; L-Lactate Dehydrogenase; Mutation, Missense; Pediococcus acidilactici

2019