Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.5.1.77	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.
3.5.1.77	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.
3.5.1.77	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

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.77	Agrobacterium sp.	-	-	-
3.5.1.77	Agrobacterium sp. KNK712	-	-	-

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Release 2023.1 (January 2023)