Page last updated: 2024-08-17

methylamine and tryptophan

methylamine has been researched along with tryptophan in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (40.00)18.2507
2000's3 (60.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ferguson, SJ; Page, MD1
Chen, ZW; Ferrari, D; Kuusk, V; Labesse, G; Mathews, FS; McIntire, WS; Rossi, GL1
Davidson, VL; Jones, LH; Pearson, AR; Tang, Y; Wilmot, CM1
Fong, RN; Inwood, WB; Kim, KS; Kustu, S; Yoshihara, C1
Biermann, N; Cavalieri, C; Einsle, O; Ferrari, D; Merli, A; Rossi, GL; Ubbink, M; Vlasie, MD1

Other Studies

5 other study(ies) available for methylamine and tryptophan

ArticleYear
Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group.
    European journal of biochemistry, 1993, Dec-01, Volume: 218, Issue:2

    Topics: Benzoquinones; Choline; Cytochrome c Group; Gram-Negative Aerobic Bacteria; Indolequinones; Methylamines; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peptides; Quinones; Tryptophan

1993
Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1.
    The Journal of biological chemistry, 1998, Oct-02, Volume: 273, Issue:40

    Topics: Bacterial Proteins; Binding Sites; Cesium; Crystallography, X-Ray; Indolequinones; Methylamines; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Tryptophan

1998
Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.
    The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17

    Topics: Aspartic Acid; Binding Sites; Crystallography, X-Ray; Cysteine; Disulfides; Indolequinones; Kinetics; Mass Spectrometry; Methylamines; Models, Chemical; Models, Molecular; Models, Statistical; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Conformation; Tryptophan

2005
The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion.
    Proceedings of the National Academy of Sciences of the United States of America, 2007, Nov-20, Volume: 104, Issue:47

    Topics: Cation Transport Proteins; Chromatography, Thin Layer; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Ions; Lysine; Methylamines; Microbial Viability; Mutation; Tryptophan

2007
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus.
    Biochemistry, 2008, Jun-24, Volume: 47, Issue:25

    Topics: Bacterial Proteins; Binding Sites; Catalysis; Copper; Crystallization; Crystallography, X-Ray; Electron Transport; Indolequinones; Kinetics; Metalloproteins; Methylamines; Models, Molecular; Molecular Weight; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Solutions; Tryptophan

2008