Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution
about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneCrystal structure of the precursor of galactose oxidase: An unusual self-processing enzymeCrystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridgesStructure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinkingIn Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase ComplexEvidence for a Dual Role of an Active Site Histidine in α-Amino-β-carboxymuconate-ε-semialdehyde DecarboxylaseProline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauGStructures of MauG in complex with quinol and quinone MADHRoles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis.Involvement of a putative [Fe-S]-cluster-binding protein in the biogenesis of quinohemoprotein amine dehydrogenase.New pathway of amine oxidation respiratory chain of Paracoccus denitrificans IFO 12442.Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin.Structure of Ca2+ release channel at 14 A resolution.Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQRoles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidaseMauG: a di-heme enzyme required for methylamine dehydrogenase maturation.A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Generation of protein-derived redox cofactors by posttranslational modification.Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Bis-Fe(IV): nature's sniper for long-range oxidation.Functionally important segments in proteins dissected using Gene Ontology and geometric clustering of peptide fragments.An analysis of reaction pathways for proton tunnelling in methylamine dehydrogenaseKinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisSuicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate.Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase.Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.Biochemistry. Remote enzyme microsurgery.Active-site residues are critical for the folding and stability of methylamine dehydrogenase.Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55.Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.Role of Tyr-288 at the dioxygen reduction site of cytochrome bo studied by stable isotope labeling and resonance raman spectroscopy.Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis.Free-Energy Landscape and Proton Transfer Pathways in Oxidative Deamination by Methylamine Dehydrogenase.The investigation of different pollutants and operation processes on sludge toxicity in sequencing batch bioreactors.Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Unusual post-translational protein modifications: the benefits of sophistication
P2860
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P2860
Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Refined crystal structure of m ...... trificans at 1.75 A resolution
@ast
Refined crystal structure of m ...... trificans at 1.75 A resolution
@en
Refined crystal structure of m ...... trificans at 1.75 A resolution
@nl
type
label
Refined crystal structure of m ...... trificans at 1.75 A resolution
@ast
Refined crystal structure of m ...... trificans at 1.75 A resolution
@en
Refined crystal structure of m ...... trificans at 1.75 A resolution
@nl
prefLabel
Refined crystal structure of m ...... trificans at 1.75 A resolution
@ast
Refined crystal structure of m ...... trificans at 1.75 A resolution
@en
Refined crystal structure of m ...... trificans at 1.75 A resolution
@nl
P2093
P356
P1476
Refined crystal structure of m ...... trificans at 1.75 A resolution
@en
P2093
P304
P356
10.1006/JMBI.1997.1511
P407
P577
1998-02-01T00:00:00Z