pyridoxamine phosphate and cysteine

pyridoxamine phosphate has been researched along with cysteine in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19904 (44.44)18.7374
1990's3 (33.33)18.2507
2000's2 (22.22)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Snell, EE; Suelter, CH1
Dobryszycki, P; Kochman, M1
Esaki, N; Karai, N; Nakamura, T; Soda, K; Tanaka, H1
Esaki, N; Karai, N; Soda, K; Tanaka, H1
Gloss, LM; Kirsch, JF1
Furumo, NC; Kirsch, JF1
Leoncini, R; Marinello, E; Pagani, R; Pizzichini, M; Terzuoli, L1
Conway, ME; Farber, GK; Hutson, SM; Yennawar, HP; Yennawar, NH1
Agnihotri, G; Liu, HW; Liu, YN; Paschal, BM1

Other Studies

9 other study(ies) available for pyridoxamine phosphate and cysteine

ArticleYear
Assay of pyridoxal phosphate and pyridoxamine phosphate, employing S-o-nitrophenyl-L-cysteine, a chromogenic substrate of tryptophanase.
    Methods in enzymology, 1979, Volume: 62

    Topics: Cysteine; Escherichia coli; Lyases; Nitrobenzenes; Organophosphorus Compounds; Pyridoxal Phosphate; Pyridoxamine; Tryptophanase

1979
Fluorescence resonance energy transfer studies on the proximity between lysine-107 and cysteine-239 in rabbit muscle aldolase.
    Biochimica et biophysica acta, 1988, Oct-12, Volume: 956, Issue:3

    Topics: 4-Chloro-7-nitrobenzofurazan; Animals; Cysteine; Energy Transfer; Fructose-Bisphosphate Aldolase; Lysine; Muscles; Protein Binding; Protein Conformation; Pyridoxal Phosphate; Pyridoxamine; Rabbits; Spectrometry, Fluorescence

1988
Mechanism of reactions catalyzed by selenocysteine beta-lyase.
    Archives of biochemistry and biophysics, 1985, May-01, Volume: 238, Issue:2

    Topics: Alanine; Animals; Binding Sites; Cysteine; In Vitro Techniques; Keto Acids; Liver; Lyases; Pyridoxamine; Selenium; Selenocysteine; Swine

1985
Reaction and regulation mechanisms of selenocysteine beta-lyase.
    Progress in clinical and biological research, 1984, Volume: 144A

    Topics: Aluminum; Animals; Cysteine; Dithiothreitol; Keto Acids; Liver; Lyases; Magnetic Resonance Spectroscopy; Pyridoxal Phosphate; Pyridoxamine; Selenium; Selenocysteine; Swine

1984
Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
    Biochemistry, 1995, Sep-26, Volume: 34, Issue:38

    Topics: Aspartate Aminotransferases; Binding Sites; Cysteine; Escherichia coli; Imines; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Protein Conformation; Pyridoxal Phosphate; Pyridoxamine; Spectrophotometry; Structure-Activity Relationship; Titrimetry

1995
Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid.
    Archives of biochemistry and biophysics, 1995, May-10, Volume: 319, Issue:1

    Topics: Aspartate Aminotransferases; Cysteine; Escherichia coli; Half-Life; Hydrogen-Ion Concentration; Indicators and Reagents; Kinetics; Models, Biological; Neurotransmitter Agents; Pyridoxamine; Quinones; Spectrophotometry

1995
The regulation of alanine and aspartate aminotransferase by different aminothiols and by vitamin B-6 derivatives.
    Biochimica et biophysica acta, 1994, Feb-16, Volume: 1204, Issue:2

    Topics: Alanine Transaminase; Aspartate Aminotransferases; Cyanates; Cysteine; Dose-Response Relationship, Drug; Hydrogen-Ion Concentration; Pyridoxal Phosphate; Pyridoxamine; Pyridoxine; Stereoisomerism; Temperature

1994
Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms.
    Biochemistry, 2002, Oct-01, Volume: 41, Issue:39

    Topics: Alanine Transaminase; Binding Sites; Crystallization; Crystallography, X-Ray; Cysteine; D-Alanine Transaminase; Escherichia coli Proteins; Humans; Isoenzymes; Isoleucine; Lysine; Mitochondria; Models, Molecular; Oxo-Acid-Lyases; Protein Conformation; Protein Structure, Secondary; Pyridoxamine; Schiff Bases; Substrate Specificity; Transaminases; Valine

2002
Identification of an unusual [2Fe-2S]-binding motif in the CDP-6-deoxy-D-glycero-l-threo-4-hexulose-3-dehydrase from Yersinia pseudotuberculosis: implication for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses.
    Biochemistry, 2004, Nov-09, Volume: 43, Issue:44

    Topics: Amino Acid Motifs; Amino Acid Sequence; Catalysis; Cysteine; Enzyme Activation; Hexoses; Hydro-Lyases; Iron; Iron-Sulfur Proteins; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Protein Binding; Pyridoxamine; Sequence Alignment; Yersinia pseudotuberculosis

2004