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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.
    Relationship between an increase in thermostability and amino acid substitution in N-carbamyl-D-amino acid amidohydrolase (1998), Biosci. Biotechnol. Biochem., 62, 1672-1675.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H57L mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
P203A mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
P203H mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
P203I mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
P203N mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
P203T mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
V236A mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
V236S mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.
V236T mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser Agrobacterium sp.

Organism

Organism UniProt Comment Textmining
Agrobacterium sp.
-
 wild type and mutant enzymes
-