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EC Number
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3.5.1.87
metabolism
the enzyme is involved in the (N-carbamoyl-L-cysteine) pathway (L-NCC pathway) converting DL-2-amino-DELTA2-thiazoline-4-carboxylic acid to L-cysteine
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,
733554
3.5.1.87
more
horseradish peroxidase (
EC 1.11.1.7
) and N-carbamoyl-L-amino acid amidohydrolase (L-N-carbamoylase,
EC 3.5.1.87
) are used as model proteins to investigate the effect of pegylationon enzyme activity and stability. Pegylation of enzymes, pegylation of L-N-carbamoylase with activated PEG2000, method evaluation, overview. Decline in activity for the pegylated L-N-carbamoylase. The modulation of enzyme activity and stability upon pegylation is generally mediated by the PEG domains in protecting active sites from freeradicals and/or in limiting the accessibility of substrates. Upon pegylation with lower molecular weight PEG the thermostability of HRP increases significantly. The enhancement in thermostability exhibited by PEG2000-HRP can thus be attributed to the stabilizing effect exhibited by the hydrophilic PEG domains of PEG-HRP conjugates in reducing aggregation of enzyme
758260
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