(Q34232400)

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Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

3

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Bernd Nidetzky

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author name string

Anita Slavica

1

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Iskandar Dib

2

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Europe PubMed Central

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31 July 2017

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publication date

1 December 2005

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Europe PubMed Central

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31 July 2017

Applied and Environmental Microbiology

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Europe PubMed Central

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31 July 2017

71

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Europe PubMed Central

PubMed publication ID

31 July 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

8061-8068

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling

1 reference

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Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II

1 reference

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Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

1 reference

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D-Amino acid oxidase: structure, catalytic mechanism, and practical application

1 reference

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Methionine oxidation and aging

1 reference

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The oxidative environment and protein damage.

1 reference

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Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases

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Application of amperometric biosensors to the determination of vitamins and alpha-amino acids

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Oxidizing enzymes as biocatalysts.

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ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

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Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

1 reference

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The reactivity and oxidation pathway of cysteine 232 in recombinant human alpha 1-antitrypsin.

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Similarity between condensed phase and gas phase chemistry: fragmentation of peptides containing oxidized cysteine residues and its implications for proteomics

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Post-translational modification is essential for catalytic activity of nitrile hydratase

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Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation

1 reference

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Mass spectrometric identification of a stable catalytic cysteinesulfinic acid residue in an enzymatically active chemically modified glucoamylase mutant

1 reference

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Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2

1 reference

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The effect on subtilisin activity of oxidizing a methionine residue

1 reference

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[37] Reaction of protein sulfhydryl groups with Ellman's reagent

1 reference

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Fluorescence-based peptide labeling and fractionation strategies for analysis of cysteine-containing peptides

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Further studies on the fragmentation of protonated ions of peptides containing aspartic acid, glutamic acid, cysteine sulfinic acid, and cysteine sulfonic acid

1 reference

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Reactive sulphur species in oxidative signal transduction.

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Fragmentation of protonated ions of peptides containing cysteine, cysteine sulfinic acid, and cysteine sulfonic acid.

1 reference

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Catalytic properties of D-amino acid oxidase in cephalosporin C bioconversion: a comparison between proteins from different sources.

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Specific modification of two tryptophans within the nuclear-encoded subunits of bovine cytochrome c oxidase by hydrogen peroxide

1 reference

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Use of physicochemical tools to determine the choice of optimal enzyme: stabilization of D-amino acid oxidase.

1 reference

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Fusion protein of Vitreoscilla hemoglobin with D-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C.

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Substitution of the critical methionine residues in trigonopsis variabilis D-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide.

1 reference

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Evidence for the functional importance of Cys298 in D-amino acid oxidase from Trigonopsis variabilis

1 reference

https://pubmed.ncbi.nlm.nih.gov/16332786

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification and localization of a stable sulfenic acid in peroxide-treated tetrachlorohydroquinone dehalogenase using electrospray mass spectrometry

1 reference

https://pubmed.ncbi.nlm.nih.gov/16332786

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of D-amino acid oxidase from Trigonopsis variabilis

1 reference

https://pubmed.ncbi.nlm.nih.gov/16332786

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/AEM.71.12.8061-8068.2005

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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