Document Detail

Assays of d: -amino Acid oxidases.
MedLine Citation:
PMID:  21956578     Owner:  NLM     Status:  In-Data-Review    
D: -Amino acid oxidase and D: -aspartate oxidase are two well-known FAD-containing flavooxidases that catalyze the same reaction (the oxidative deamination) on different D: -amino acids. D: -aspartate oxidase is specific for acidic D: -amino acids (i.e., D: -aspartate and D: -glutamate) and D: -amino acid oxidase is active on neutral and polar D: -amino acids (a low activity is also detected on basic D: -amino acids). The assay of these flavoenzymes is of utmost importance in different fields because D: -amino acids are common constituents of bacterial cell walls, are present in foods and because free D: -serine and D: -aspartic acid were identified in brain and peripheral tissues of mammals. In this chapter, we report on the most used methods employed to assay the activity of D: -amino acid oxidase and D: -aspartate oxidase. Interestingly, their activity can be followed using different assays, namely D: -amino acid or oxygen consumption, α-keto acid or ammonia production, or using artificial dyes as final indicator of the flavin redox reaction.
Gabriella Tedeschi; Loredano Pollegioni; Armando Negri
Related Documents :
21995488 - Contribution of glutamate decarboxylase in lactobacillus reuteri to acid resistance and...
12239128 - Goldfish ghrelin: molecular characterization of the complementary deoxyribonucleic acid...
18155628 - Solid state 19f nmr parameters of fluorine-labeled amino acids. part ii: aliphatic subs...
19068478 - Trna-independent pretransfer editing by class i leucyl-trna synthetase.
8205388 - Purification and characterization of vitellin-2 from the ovary of the american cockroac...
16190738 - Chemical synthesis of 23 kda glycoprotein by repetitive segment condensation: a synthes...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Methods in molecular biology (Clifton, N.J.)     Volume:  794     ISSN:  1940-6029     ISO Abbreviation:  Methods Mol. Biol.     Publication Date:  2012  
Date Detail:
Created Date:  2011-09-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9214969     Medline TA:  Methods Mol Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  381-95     Citation Subset:  IM    
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria - sez. Biochimica, Università degli Studi di Milano, Milano, Italy,
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Assay of amino Acid racemases.
Next Document:  Enzymes acting on d: -amino Acid containing peptides.