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Example sentences for: hydrolyze
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There are over 300 distinct β-lactamases known, and these enzymes have been grouped by a number of classification schemes [ 8 9 10 11 12 13 14 15 ] . For example, Bush has developed a scheme, based on the enzymes' molecular properties, that has four distinct β-lactamase groups [ 10 15 ] . One of the more alarming groups are the Bush group 3 enzymes, which are Zn(II) dependent enzymes that hydrolyze nearly all known β-lactam containing antibiotics and for which there are no or very few known clinical inhibitors [ 9 14 16 17 18 19 ] . The metallo-β-lactamases have been further divided by Bush into subgroups based on amino acid sequence identity: the Ba enzymes share a >23% sequence identity, require 2 Zn(II) ions for full activity, prefer penicillins and cephalosporins as substrates, and are represented by metallo-β-lactamase CcrA from Bacteroides fragilis, the Bb enzymes share a 11% sequence identity with the Ba enzymes, require only 1 Zn(II) ion for full activity, prefer carbapenems as substrates, and are represented by the metallo-β-lactamase imiS from Aeromonas sobria, and the Bc enzymes have only 9 conserved residues with the other metallo-β-lactamases, require 2 Zn(II) ions for activity, contain a different metal binding motif than the other metallo-β-lactamases, prefer penicillins as substrates, and are represented by the metallo-β-lactamase L1 from Stenotrophomonas maltophilia [ 9 ] . A similar grouping scheme (B1, B2, and B3) based on structural properties of the metallo-β-lactamases has recently been offered [ 41 ] . The diversity of the group 3 β-lactamases is best exemplified by the enzymes' vastly differing efficacies towards non-clinical inhibitors; these differences predict that one inhibitor may not inhibit all metallo-β-lactamases [ 18 20 21 22 23 24 25 26 27 28 29 ] . To combat this problem, we are characterizing a metallo-β-lactamase from each of the subgroups in an effort to identify a common structural or mechanistic aspect of the enzymes that can be targeted for the generation of an inhibitor.
All characterized members of this family are peptidases, and they either hydrolyze the D-γ-glutamyl-meso-diaminopimelate linkage or N -acetylmuramate- L-alanine linkage [ 19, 25].
The subunit A protein is approximately 70 kDa in most organisms studied and is a hydrophilic peptide located in the head group of the V 1 peripheral sector in three copies per holoenzyme [ 18 ] . This subunit contains a nucleotide binding motif and functions to bind and hydrolyze ATP [ 19 ] . In addition, subunit A contains a highly conserved cysteine residue located within the enzymes' catalytic center that may be involved in regulation of the holoenzyme [ 20 21 22 23 ] . Cloning, sequencing and characteristics of subunit A of the V-Type ATPase from Arabidopsis thaliana have been previously reported [ 24 ] .
In these processes the wall is disassembled through the action of a diverse set of enzymes that hydrolyze various linkages in peptidoglycan.
Streptococcus mutans in which DCP is inactive do not initiate growth at below pH 6.5 and make glycerol LTA without D-alanine [ 14 ] . In the DCP active strains, soluble D-Alanyl LTA is extruded into culture fluid in vitro [ 16 17 ] or plaque in vivo [ 18 ] . The D-alanyl esters are stable at pH 6.0 at 37°C, but hydrolyze to free D-alanine and LTA with a half-life of 3.9 h at pH 8.0 [ 19 ] . Healthy gingival sulci have a pH of 6.5 - 7.5 and inflamed sulci a pH of 7.5-8.
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