Metallo-beta-lactamases are zinc enzymes able to hydrolyze the four-membered ring of beta-lactam antibiotics, representing one of the latest generations of beta-lactamases. These enzymes belong to the zinc metallo-hydrolase family of the beta-lactamase fold. Enzymes belonging to this family have a bimetallic active site whose structure varies among different members by point substitutions of th...

Carbonic anhydrases (CAs, EC 4) are zinc containing metalloenzymes. The active site of these enzymes contains a Zn (II) ion Co-ordinated by three histidine residues and a water molecule/hydroxide ion. Four distinct gene families encode them and distributed throughout the phylogenetic tree. Presently 16 different CA isoforms of alpha family have been isolated and characterized in mammals. They c...

Differential mRNA display was used to comprehensively screen the murine thymic transcriptome for genes modulated in vivo by dietary zinc. A moderate feeding protocol rendered young adult, outbred mice zinc-deficient and zinc-supplemented without alterations in feeding behavior or growth. However, these levels of deficiency and supplementation altered specific mRNA abundances in a manner detecta...

tial element for more than a hundred years, ever since it was discovered by Raulin in 1869 to be required for the growth of Aspergillus niger. However, it has not been until relatively modern times that the universal importance of this metal for both human and animal health became fully appreciated. To date more than 200 zinc dependent enzymes have actually been identified in all the main bioch...

TrzN, the broad-specificity triazine hydrolase from Arthrobacter and Nocardioides spp., is reportedly in the amidohydrolase superfamily of metalloenzymes, but previous studies suggested that a metal was not required for activity. To help resolve that conundrum, a double chaperone expression system was used to produce multimilligram quantities of functionally folded, recombinant TrzN. The TrzN o...

Metallochaperones function as intracellular shuttles for metal ions. At present, no evidence for the existence of any eukaryotic zinc-chaperone has been provided although metallochaperones could be critical for the physiological functions of Zn2+ metalloenzymes. We propose that the complex formed in skeletal muscle by the Zn2+ metalloenzyme AMP deaminase (AMPD) and the metal binding protein his...

The role of zinc in the catalytic action of yeast alcohol dehydrogenase has been studied through the kinetics of the inhibition of activity by chelating agents (I), particularly l,lO-phenanthroline (2-4). In aqueous solution the complexes of 1, lo-phenanthroline with Zn++ ions exhibit characteristic absorption spectra, as do the complexes of this agent with the zinc atoms of yeast alcohol dehyd...

Carbonic anhydrases are mostly zinc metalloenzymes that catalyze the reversible hydration/dehydration of CO2/HCO3 (-) Previously, the X-ray crystal structures of CO2-bound holo (zinc-bound) and apo (zinc-free) human carbonic anhydrase IIs (hCA IIs) were captured at high resolution. Here, we present sequential timeframe structures of holo- [T = 0 s (CO2-bound), 50 s, 3 min, 10 min, 25 min, and 1...