4LF0
 
 | | The E142D mutant of the amidase from Geobacillus pallidus | | Descriptor: | Aliphatic amidase | | Authors: | Sewell, B.T, Weber, B.W, Kimani, S.W, Cowan, D.A, Hunter, R, Venter, G.A, Gumbart, J.C, Thuku, R.N, Varsani, A. | | Deposit date: | 2013-06-26 | | Release date: | 2013-08-21 | | Last modified: | 2024-03-20 | | Method: | X-RAY DIFFRACTION (1.1 Å) | | Cite: | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
J.Biol.Chem., 288, 2013
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4GYN
 | | The E142L mutant of the amidase from Geobacillus pallidus | | Descriptor: | Aliphatic amidase, CHLORIDE ION | | Authors: | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | | Deposit date: | 2012-09-05 | | Release date: | 2013-08-21 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
J.Biol.Chem., 288, 2013
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4GYL
 | | The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine | | Descriptor: | Aliphatic amidase, CHLORIDE ION, PROPIONAMIDE | | Authors: | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | | Deposit date: | 2012-09-05 | | Release date: | 2013-08-21 | | Last modified: | 2014-02-05 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
J.Biol.Chem., 288, 2013
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4KZF
 | | The mechanism of the amidases: The effect of the mutation E142L in the amidase from Geobacillus pallidus | | Descriptor: | Aliphatic amidase, CHLORIDE ION | | Authors: | Weber, B.W, Sewell, B.T, Kimani, S.W, Varsani, A, Cowan, D.A, Hunter, R. | | Deposit date: | 2013-05-29 | | Release date: | 2013-08-21 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.85 Å) | | Cite: | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
J.Biol.Chem., 288, 2013
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