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Literature summary for 3.5.1.77 extracted from

  • Ikenaka, Y.; Nanba, H.; Yajima, K.; Yamada, Y.; Takano, M.; Takahashi, S.
    Increase in thermostability of N-carbamyl-D-amino acid amidohydrolase on amino acid substitutions (1998), Biosci. Biotechnol. Biochem., 62, 1668-1671.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H57Y mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme Agrobacterium sp.
P203L mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme Agrobacterium sp.
P203S mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme Agrobacterium sp.

Organism

Organism UniProt Comment Textmining
Agrobacterium sp.
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Agrobacterium sp. KNK712
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