Novel cofactors via post-translational modifications of enzyme active sites.
about
Crystal 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-bridgesThe Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis † , ‡Function and Structure of a Prokaryotic Formylglycine-generating EnzymeCross-Link Formation of the Cysteine 228−Tyrosine 272 Catalytic Cofactor of Galactose Oxidase Does Not Require Dioxygen † ‡Structural Insights into the Recovery of Aldolase Activity inN-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis StrategyAddition of the keto functional group to the genetic code of Escherichia coli.Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.Homemade cofactors: self-processing in galactose oxidase.Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxinEvolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases.Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediateMauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.Chemoproteomic profiling and discovery of protein electrophiles in human cells.Generation of protein-derived redox cofactors by posttranslational modification.Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway.Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity.The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase.Second-Order Biomimicry: In Situ Oxidative Self-Processing Converts Copper(I)/Diamine Precursor into a Highly Active Aerobic Oxidation Catalyst.A metalloantibody that irreversibly binds a protein antigen.Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.Unusual post-translational protein modifications: the benefits of sophistication
P2860
Q27636072-4442725F-C50F-46F3-8557-5D108ABA57B7Q27636140-05841226-612D-460E-ACEA-1077A6830627Q27644234-3CBF717D-CAE2-4B97-BE34-B4D212E8C5CEQ27650231-A6FAF516-D090-47F2-92A9-9D86A328D5DAQ27651979-70758A30-3714-4308-B875-0B81BB39DC6AQ27676442-0FEF9B56-D8B0-4FDC-B234-EA0089063151Q30332382-E49E12D9-31DC-4C54-8ABF-A176E9A31FADQ30360723-899D1DCE-5760-418B-81B7-EC7948664CADQ33948866-4F1C15B9-16A4-4EDC-9486-D8776EC780ECQ34426006-030019A7-ECD9-45BE-BC17-741EC54FD451Q34592277-13393B25-2AE0-427C-BBF8-45ADC762982EQ35824616-C9E011B4-5BC5-48B6-A6AD-1EB7BCF92BBFQ36592463-6F527D5E-B3A3-48E8-B07D-EF74714CC0D5Q37359679-FDA950A5-B062-4DB5-BDCF-66A5C17A843CQ37664926-A247FC02-3C1C-47A7-A396-038264EE5F40Q37799264-1E8A4FB1-CC38-4B53-9B10-E2886C2B9094Q38290367-EE23208B-07E9-4B32-95E3-A638C6EA9E69Q39119961-CA1F2706-AB14-44F2-8CE1-8E2A41C9BB35Q40007786-C2AE8BF0-6921-4585-B4F3-D996FBFCE694Q41856272-C8E6120E-176D-4F5F-80AA-724E56DDCA57Q42119335-BE89123C-B766-40C4-9413-4460CC2FB7FEQ42290284-59345D44-7D56-480D-BC06-091CF3BF6E4EQ43808918-52D346CB-67E7-4A6C-836F-ACD43532F5C5Q45285252-C3BECFB9-6720-4CB5-B803-E69263D099A7Q57810667-46B70FE9-32BB-4621-877E-8EB32FC70B14
P2860
Novel cofactors via post-translational modifications of enzyme active sites.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Novel cofactors via post-translational modifications of enzyme active sites.
@ast
Novel cofactors via post-translational modifications of enzyme active sites.
@en
type
label
Novel cofactors via post-translational modifications of enzyme active sites.
@ast
Novel cofactors via post-translational modifications of enzyme active sites.
@en
prefLabel
Novel cofactors via post-translational modifications of enzyme active sites.
@ast
Novel cofactors via post-translational modifications of enzyme active sites.
@en
P1476
Novel cofactors via post-translational modifications of enzyme active sites.
@en
P2093
van der Donk WA
P304
P356
10.1016/S1074-5521(00)00140-X
P577
2000-07-01T00:00:00Z