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Literature summary for 3.5.1.77 extracted from

  • Nakai, T.; Hasegawa, T.; Yamashita, E.; Yamamoto, M.; Kumasaka, T.; Ueki, T.; Nanba, H.; Ikenaka, Y.; Takahashi, S.; Sato, M.; Tsukihara, T.
    Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases (2000), Structure, 8, 729-738.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapour-diffusion method. Native crystals belong to space group P2(1)2(1)2 with a = 67.84 A, b = 137.83 A, c = 68.39 A. Structure determined to 1.7 A resolution. The enzyme forms a homotetramer and each monomer consists of a variant of the alpha + beta fold. The topology of the enzyme comprises a sandwich of parallel beta sheets surrounded by two layers of alpha helices Agrobacterium sp.

Organism

Organism UniProt Comment Textmining
Agrobacterium sp.
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Agrobacterium sp. KNK712
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer Agrobacterium sp. ?
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 ?
additional information D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer Agrobacterium sp. KNK712 ?
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 ?