3545-78-6Relevant articles and documents
Does N-hydroxyglycine inhibit plant and fungal laccases?
Zhang, Jingming,Kjonaas, Richard,Flurkey, William H.
, p. 775 - 783 (1999)
The effect of N-hydroxyglycine on the oxidation of substrates, syringaldazine, tolidine, 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol, by fungal and plant laccases was examined. At μM concentrations, N-hydroxyglycine decolorized solutions of substrates oxidized enzymatically by laccase or chemically by sodium periodate. This discoloration, or bleaching, could be mistaken for inhibition of laccase activity if N-hydroxyglycine was added to assays for laccase that monitored colored products, N-hydroxyglycine also affected oxygen consumption assays when some of these substrates were oxidized enzymatically or chemically. Spectral scans of the products formed during enzymatic or chemical oxidation of the substrates indicated that addition of N-hydroxyglycine caused a general decrease in absorption. Except for 2,6-dimethoxyphenol, no formation of new absorption peaks was noted. These results suggest that N- hydroxyglycine may not be a 'classical' enzyme inhibitor of laccase, but that this compound interferes with both spectrophotometric and oxygen uptake enzyme assays for laccase.
An improved synthesis of N-hydroxyamino acids and their esters using (Z)-2-furaldehyde oxime
Goto,Kawakita,Okutani,Miki
, p. 3202 - 3207 (2007/10/02)
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N-hydroxyamino acids. Irreversible inhibitors of pyridoxal 5'-phosphate enzymes and substrates of D- and L-amino acid oxidases
Cooper,Griffith
, p. 2748 - 2753,2749,2753 (2007/10/04)
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