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Literature summary for 3.5.1.87 extracted from

  • Hsieh, Y.; Lin, S.
    Effect of PEGylation on the activity and stability of horseradish peroxidase and L-N-carbamoylase in aqueous phases (2015), Process Biochem., 50, 1372-1378 .
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
gene lnc, recombinant expression of His-tagged enzyme in Escherichia coli Geobacillus kaustophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-carbamoyl-L-homophenylalanine + H2O Geobacillus kaustophilus
-
 L-homophenylalanine + NH3 + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Geobacillus kaustophilus Q8GQG5 i.e. Bacillus kaustophilus
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis Geobacillus kaustophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-carbamoyl-L-homophenylalanine + H2O
-
 Geobacillus kaustophilus L-homophenylalanine + NH3 + CO2
-
 ?

Synonyms

Synonyms Comment Organism
L-N-carbamoylase
-
 Geobacillus kaustophilus
Lnc
-
 Geobacillus kaustophilus

General Information

General Information Comment Organism
additional information 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 Geobacillus kaustophilus