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3.5.1.11: penicillin amidase

This is an abbreviated version!
For detailed information about penicillin amidase, go to the full flat file.

Word Map on EC 3.5.1.11

Reaction

penicillin
+
H2O
=
a carboxylate
 +
6-aminopenicillanate

Synonyms

ACPGA001 PGA, AfPGA, alpha-acylamino-beta-lactam acylhydrolase, amidase, amidohydrolase, ampicillin acylase, AuAAC, benzylpenicillin acylase, BmPGA, Eca3205, KcPGA, maPGA, More, novozym 217, PA, PAC, penicillin acylase, penicillin amidase, Penicillin amidohydrolase, penicillin G acylase, Penicillin G amidase, Penicillin G amidohydrolase, penicillin V acylase, Penicillin V amidase, penicillin-G acylase, PGA, PGA650, PVA, semacylase, Sm-PVA, YxeI

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.11 penicillin amidase

Crystallization

Crystallization on EC 3.5.1.11 - penicillin amidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparative modeling of structure
-
purified enzyme, hanging drop vapour diffusion method, method optimization, from crystallization solution consisting of 15% w/v PEG 8000, 0.1 M Tris-HCl, pH 7.5, and 0.5% w/v beta-octyl-glucopyranoside solution. The presence of 0.06 ml beta-octyl-glucopyranoside in the well solution leads to orthorhombic crystals, whereas 0.1 ml beta-octyl-glucopyranoside result in tetragonal crystals, X-ray diffraction structure determination and analysis at A resolution at 3.3-3.5 A resolution, molecular replacement method
both wild-type and mutants F146Y, F24Y, F146Y/F24Y
-
crystals of space group P1 diffracted to beyond 2.3 A
-
hanging-drop vapour diffusion at 18°C, crystal structure of a slowly processing precursor mutant T263G
-
crystals of both mutants S1C and S1G belong to space group P1 with four molecules in the asymmetric unit. The three-dimensional structures of these mutants are refined at resolutions 2.8 A and 2.5 A, respectively. Comparison of the structures with similar structures of Escherichia coli PGA (EcPGA) reveals various conformational changes that lead to autocatalytic processing and consequent removal of the spacer peptide
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 300 nl of 45 mg/ml protein solution with 0.1 ml of precipitant solution containing 30% w/v PEG 4000, 50 mM sodium cacodylate pH 5.6, 0.5 M potassium thiocyanate, 3-4 days, mixing of 500 nl of protein and of precipitant solutions each results in crystals that grow in a week under a wide range of pH conditions using 50 mM sodium cacodylate buffer, method optimization, X-ray diffraction structure determination and analysis at 2.5-3.5 A resolution, molecular replacement method
mature inactive mutants C1S, C1A, N175D and their precursor forms
-
sitting drop vapor diffusion method at 22°C, crystal structure at 2.5 A resolution
2.5 A resolution, R-factor 0.154, R-free 0.165
-