ArticleBiochemistry2007
The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 108 citations in OpenAlex.
- Structural enzymology of a Fusarium graminearum aldehyde oxidase reveals a distinct active-site and reactivity versus its paralog galactose oxidase.The Biochemical journal · 2026Article
- Hangman dipyrrin complexes.Chemical science · 2026Article
- Expansion of Auxiliary Activity Family 5 sequence space via biochemical characterization of six new copper radical oxidases.Applied and environmental microbiology · 2024Article
- Copper-radical oxidases: A diverse group of biocatalysts with distinct properties and a broad range of biotechnological applications.Engineering microbiology · 2022Review
- Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase.ACS catalysis · 2022Article
- Aglycone sterics-selective enzymatic glycan remodeling.iScience · 2022Article
- π-π Stacking Interaction of Metal Phenoxyl Radical Complexes.Molecules (Basel, Switzerland) · 2022Review
- A survey of substrate specificity among Auxiliary Activity Family 5 copper radical oxidases.Cellular and molecular life sciences : CMLS · 2021Article
- A Putative Lignin Copper Oxidase fromJournal of fungi (Basel, Switzerland) · 2021Article
- Two Fusarium copper radical oxidases with high activity on aryl alcohols.Biotechnology for biofuels · 2021Article
- Production of Galactose Oxidase Inside the Fusarium fujikuroi Species Complex and Recombinant Expression and Characterization of the Galactose Oxidase GaoA Protein from Fusarium subglutinans.Molecular biotechnology · 2019Article
- Time-Resolved Infrared and Visible Spectroscopy on Cryptochrome aCRY: Basis for Red Light Reception.Biophysical journal · 2019Article
- RUBY, a Putative Galactose Oxidase, Influences Pectin Properties and Promotes Cell-To-Cell Adhesion in the Seed Coat Epidermis of Arabidopsis.The Plant cell · 2019Article
- A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family.PloS one · 2019Article
- Characterization of the one-electron oxidized Cu(II)-salen complexes with a side chain aromatic ring: the effect of the indole ring on the Cu(II)-phenoxyl radical species.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.Protein science : a publication of the Protein Society · 2017Article
- Structure of the Reduced Copper Active Site in Preprocessed Galactose Oxidase: Ligand Tuning for One-Electron OJournal of the American Chemical Society · 2016Article
- Influence of a family 29 carbohydrate binding module on the recombinant production of galactose oxidase in Pichia pastoris.Data in brief · 2016Article
- Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family.Nature communications · 2015Article
- Defining the role of tyrosine and rational tuning of oxidase activity by genetic incorporation of unnatural tyrosine analogs.Journal of the American Chemical Society · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 1 institution in 2 countries.
Funding
Abstract
The function of the stacking tryptophan, W290, a second-coordination sphere residue in galactose oxidase, has been investigated via steady-state kinetics measurements, absorption, CD and EPR spectroscopy, and X-ray crystallography of the W290F, W290G, and W290H variants. Enzymatic turnover is significantly slower in the W290 variants. The Km for D-galactose for W290H is similar to that of the wild type, whereas the Km is greatly elevated in W290G and W290F, suggesting a role for W290 in substrate binding and/or positioning via the NH group of the indole ring. Hydrogen bonding between W290 and azide in the wild type-azide crystal structure are consistent with this function. W290 modulates the properties and reactivity of the redox-active tyrosine radical; the Y272 tyrosyl radicals in both the W290G and W290H variants have elevated redox potentials and are highly unstable compared to the radical in W290F, which has properties similar to those of the wild-type tyrosyl radical. W290 restricts the accessibility of the Y272 radical site to solvent. Crystal structures show that Y272 is significantly more solvent exposed in the W290G variant but that W290F limits solvent access comparable to the wild-type indole side chain. Spectroscopic studies indicate that the Cu(II) ground states in the semireduced W290 variants are very similar to that of the wild-type protein. In addition, the electronic structures of W290X-azide complexes are also closely similar to the wild-type electronic structure. Azide binding and azide-mediated proton uptake by Y495 are perturbed in the variants, indicating that tryptophan also modulates the function of the catalytic base (Y495) in the wild-type enzyme. Thus, W290 plays multiple critical roles in enzyme catalysis, affecting substrate binding, the tyrosyl radical redox potential and stability, and the axial tyrosine function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.