Bacteria hydrolytic

The antibacterial effectiveness of penicillins cephalospotins and other P-lactam antibiotics depends upon selective acylation and consequentiy, iaactivation, of transpeptidases involved ia bacterial ceU wall synthesis. This acylating ability is a result of the reactivity of the P-lactam ring (1). Bacteria that are resistant to P-lactam antibiotics often produce enzymes called P-lactamases that inactivate the antibiotics by cataly2ing the hydrolytic opening of the P-lactam ring to give products (2) devoid of antibacterial activity. 

Brief notes are added on phosphorofluoridates even though their destruction by microbial activity— though clearly possible—is limited by their toxicity to the requisite microorganisms. One of the motivations for their inclusion is the fact that the hydrolytic enzyme(s) responsible for defluorination—organophosphorus acid anhydrase (OPA)—is widespread, and is found in a number of bacteria (Landis and DeFrank 1990). The microbial hydrolysis of organophosphorus pesticides and cholinesterase inhibitors is accomplished by several distinct enzymes, which are collectively termed organophosphorus acid anhydrases (OPAs). These have been reviewed (DeFrank 1991), so that only a few additional comments are necessary. 

The bacteria in the intestinal tract serve as another well-known source of luminal drug degradation [61], though this is only important for the colon region as the luminal concentration of bacteria is 104 to 109-fold higher in the colon compared with the small intestine. Thus, this aspect is only relevant for drugs that reach this region, for example, due to poor permeability, slow dissolution or delivery by modified-release formulations. Hydrolytic and other reductive reactions are predominantly mediated by bacterial enzymes, and a list of the most prominent types... 

The decrease of peak numbers was observed, when the spectra of the same amounts of fresh (12 weeks old) and aged (9 months old) mortars were compared. This decrease might be caused by activity of ubiquitous microorganisms that live on the mortar surfaces in biofilms. Especially in mild climate conditions, algae and cyanobacteria [35] can appear here moulds (Aspergillus, Penicillium, Fusarium, Mucor) [36] and bacteria (Arthrobacter Bacillus, Micrococcus, Staphylococcus) [37,38] have been discovered as well. The microorganisms secrete various hydrolytic enzymes that can decompose the organic additives, namely proteins, and make their sample identification less sensitive... 

Although hydrolytic enzymes, esterases and amidases, are named after their major substrates, the same enzyme can often hydrolyze esters, thioesters, and amides therefore, the differentiation between esterases and amidases is sometimes artificial. The highest hydrolytic activity is in the liver, but the enzyme pseudocholinesterase is found in the serum. Gut bacteria also contain hydrolytic enzymes. 

The dried bacteria also contain invertase and this hydrolytic enzyme competes with the sucrose phosphorylase for sucrose. However, it is possible to eliminate most of the invertase from the bacterial preparations by several precipitations with ammonium sulfate. Using a partially purified sucrose phosphorylase preparation and a mixture of... 

Enzymes that perform the same catalytic function are known as homologous enzymes and fall into two classes. Heteroenzymes are derived from different sources and although they catalyse the same reaction they show different physical and kinetic characteristics. The hydrolytic enzyme a-amylase (EC 3.2.1.1) is found in the pancreatic secretion in man and is different from the enzymes of the same name which are derived from bacteria or malt. Iso-enzymes, sometimes referred to as isozymes, are different molecular forms of the same enzyme and are found in the same animal or organism although they often show a pattern of distribution between tissues. 

Antibacterial sulfonamides contain two N-atoms, the sulfonamido (N1) and the para primary amino (N4). The sulfonamido group, in contrast to a carboxamido group, is chemically and metabolically stable. In other words, hydrolytic cleavage of sulfonamides to produce a sulfonic acid and an amine has never been observed. We, therefore, focus our discussion on the primary amino group, acetylation of which is one of the major metabolic pathways for some sulfonamides. Hydrolysis of the N4-acety luted metabolites back to the parent sulfonamide can occur in the liver, kidney, and intestinal tract. The reaction is strongly influenced by the structure of the parent amine e.g., N4-acetylsulfisoxazole (4.121) was deacetylated by intestinal bacteria whereas /V4-acctyIsulI anilamide (4.122) under identical conditions was not [78][79],... 

Enteric bacterial pathogens must maneuver through a lengthy stretch of hazardous terrain before they reach their intended target or infection site within a host. Initially, they must tolerate salivary enzymes having various hydrolytic activities in the mouth, followed by exposure to shedded epithelial cells in the esophagus that may prevent local bacterial adherence (Pearson and Brownlee, 2005). In the stomach, bacteria must endure another severe environment created by the secretion of digestive enzymes and hydrochloric acid (up to 0.1 M concentration and a pH as low as 1.0). Once bacteria reach the intestines, they then encoimter mechanical. 

Irreversible hydrolytic cleavage of nucleosides catalysed by hydrolases has been observed in bacteria but not in mammalian cells [46]. 

A study on tire storage stability of penicillin G in milk showed that about 60% could be destroyed within 48 h at 2 C, while 75% could be destroyed at 22 C (22). The loss of penicillin G was attributed to the hydrolytic activity of tlie enzyme -lactamase produced by both gram-negative and gram-positive bacteria of the raw milk. This was confirmed by analogous experimentation with UHT milk, in which penicillin G did not show any decrease under mentioned storage conditions. 

---