4GYL

The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine

Summary for 4GYL

• Entry DOI: 10.2210/pdb4gyl/pdb
• Related: 4GYN
• Descriptor: Aliphatic amidase, PROPIONAMIDE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: amidase, catalytic tetrad, amidase mechanism, acrylamide, michael adduct, hydrolase
• Biological source: Bacillus sp.
• Total number of polymer chains: 1
• Total formula weight: 38733.42

Authors

Weber, B.W.,Sewell, B.T.,Kimani, S.W.,Varsani, A.,Cowan, D.A.,Hunter, R. (deposition date: 2012-09-05, release date: 2013-08-21, Last modification date: 2014-02-05)

• Primary citation: Weber, B.W.,Kimani, S.W.,Varsani, A.,Cowan, D.A.,Hunter, R.,Venter, G.A.,Gumbart, J.C.,Sewell, B.T.; The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.; J.Biol.Chem., 288:28514-28523, 2013; PubMed: 23946488; DOI: 10.1074/jbc.M113.503284

Experimental method

X-RAY DIFFRACTION (1.9 Å)