<p>Active site structure homology between (A) recombinant molinate hydrolase and (B) subtype IV amidohydrolase <i>N</i>-acetyl glucosamine-6-phosphate deacetylase from <i>T</i>. <i>maritima</i> (PDB entry: 1o12; 6). Water molecules are represented as red spheres, zinc as an orange sphere and iron as a yellow sphere.</p
The high resolution crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and t...
<p>A) Conserved active-site localization for eight proteins adopting the metallo-β-lactamase fold (P...
Muconate lactonizing enzyme (MLE), a component of the -ketoadipate pathway of Pseudomonas putida, is...
<p>The monomers are coloured individually and the zinc cofactors are represented by orange spheres.<...
<p>Overlay of the β-strands around the catalytic metal of molinate hydrolase (pink) and N-acetyl glu...
<p>The anomalous difference map computed from the diffraction data measured at the Zinc absorption e...
The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically act...
<p>(a) Superposition of apo DHNTPase (green), Ni-bound (magenta), and Co-bound (blue) structures fro...
The amidohydrolase superfamily has remarkable functional diversity, with considerable structural and...
<p><b>A</b> Superimposition of the active site regions in MtPncA (in green) and PhPncA (in red). The...
<p>(A) Superposition of the cartoon representations of <i>Pp</i>AlgJ<sub>75–370</sub> (blue) and <i>...
The LmbE-like superfamily is comprised of a series of enzymes that use a single catalytic metal ion ...
<p>A network of direct and water-mediated interactions between (L)-malate and enzyme residues and Mg...
In this paper we provide a detailed biochemical and structural characterization of the active site o...
The metallo--lactamase superfamily comprises a remarkable set of enzymes that catalyse the hydrolysi...
The high resolution crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and t...
<p>A) Conserved active-site localization for eight proteins adopting the metallo-β-lactamase fold (P...
Muconate lactonizing enzyme (MLE), a component of the -ketoadipate pathway of Pseudomonas putida, is...
<p>The monomers are coloured individually and the zinc cofactors are represented by orange spheres.<...
<p>Overlay of the β-strands around the catalytic metal of molinate hydrolase (pink) and N-acetyl glu...
<p>The anomalous difference map computed from the diffraction data measured at the Zinc absorption e...
The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically act...
<p>(a) Superposition of apo DHNTPase (green), Ni-bound (magenta), and Co-bound (blue) structures fro...
The amidohydrolase superfamily has remarkable functional diversity, with considerable structural and...
<p><b>A</b> Superimposition of the active site regions in MtPncA (in green) and PhPncA (in red). The...
<p>(A) Superposition of the cartoon representations of <i>Pp</i>AlgJ<sub>75–370</sub> (blue) and <i>...
The LmbE-like superfamily is comprised of a series of enzymes that use a single catalytic metal ion ...
<p>A network of direct and water-mediated interactions between (L)-malate and enzyme residues and Mg...
In this paper we provide a detailed biochemical and structural characterization of the active site o...
The metallo--lactamase superfamily comprises a remarkable set of enzymes that catalyse the hydrolysi...
The high resolution crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and t...
<p>A) Conserved active-site localization for eight proteins adopting the metallo-β-lactamase fold (P...
Muconate lactonizing enzyme (MLE), a component of the -ketoadipate pathway of Pseudomonas putida, is...