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Literature summary for 3.5.1.77 extracted from

  • Wang, W.C.; Hsu, W.H.; Chien, F.T.; Chen, C.Y.
    Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft (2001), J. Mol. Biol., 306, 251-261.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method, crystals belong to space group P2(1) with unit cell dimensions a = 70.23 A, b = 67.53 A, c = 137.48 A and beta = 96.12°. There are 4 molecules per asymmetric unit Agrobacterium tumefaciens

Protein Variants

Protein Variants Comment Organism
H129A inactive mutant enzyme Agrobacterium tumefaciens
H129N inactive mutant enzyme Agrobacterium tumefaciens
H129R inactive mutant enzyme Agrobacterium tumefaciens
H144A 5% of the activity of wild-type enzyme Agrobacterium tumefaciens
H215A 17% of the activity of wild-type enzyme Agrobacterium tumefaciens

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
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-
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Purification (Commentary)

Purification (Comment) Organism
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Agrobacterium tumefaciens