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Literature summary for 3.5.1.77 extracted from

  • Nanba, H.; Ikenaka, Y.; Yamada, Y.; Yajima, K.; Takano, M.; Ohkubo, K.; Hiraishi, Y.; Yamada, K.; Takahashi, S.
    Immobilization of N-carbamyl-D-amino acid amidohydrolase (1998), Biosci. Biotechnol. Biochem., 62, 1839-1844.
    View publication on PubMed

General Stability

General Stability Organism
high thermal stability and high stability in repeated batch reactions of the immobilized enzyme Pseudomonas sp.
immobilized enzyme is most stable at pH 7.0 Agrobacterium sp.
immobilized enzyme is stabilized by dithiothreitol, L-Cys, cysteamine, and sodium hydrosulfite. After 14times repeated reactions, the remaining activity of the immobilized enzyme cross-linked with 0.1% and 0.2% of glutaraldehyde, and 0.2% of the glutaraldehyde with dithiothreitol in the reaction mixture is 12%, 18%, and 63% respectively Agrobacterium sp.

Organism

Organism UniProt Comment Textmining
Agrobacterium sp.
-
-
-
Agrobacterium sp.
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expressed in Escherichia coli
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Agrobacterium sp. KNK712
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-
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Pseudomonas sp.
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strain KNK003A and strain KNK505
-

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
immobilized enzyme is most stable at pH 7.0 Agrobacterium sp.