Disease relevance of Penicin

• With E. coli cephaloridine was a poorer inducer of beta-lactamase than were the antagonized antibiotic and 6-aminopenicillanic acid [1].
• Cell surface changes in Pseudomonas aeruginosa PAO4069 in response to treatment with 6-aminopenicillanic acid [2].
• The method is based on the use of Serratia marcescens sensitive to 6-aminopenicillanic acid but comparatively resistant to benzylpenicillin [3].
• N-(functionalized alkyl) derivatives of 6-aminopenicillanic acid: a new series of specific inhibitors of beta-lactamase from Enterobacter cloacae P99 [4].
• Effect of nalidixic acid on the conversion of Staphylococcus aureus cells to L-forms in a liquid medium with 6-aminopenicillanic acid and lysozyme [5].

Psychiatry related information on Penicin

• 6-Aminopenicillanic acid in the reaction mixture was observed to be stable during conversion reactions which were carried out at both temperatures [6].

High impact information on Penicin

• The present paper presents a steady-state kinetic analysis of the inhibition of depsipeptide hydrolysis by sodium benzylpenicilloate, methyl benzylpenicilloate, 6-aminopenicillanic acid, and 7-aminocephalosporanic acid [7].
• Involvement of Escherichia coli penicillin-binding proteins (PBPs) in induction of the cloned ampC Citrobacter freundii beta-lactamase by 6-aminopenicillanic acid was investigated [8].
• Application of the fluorescamine reaction with 6-aminopenicillanic acid to estimation and detection of penicillin acylase activity [9].
• Acyltransferase activity from Escherichia coli producing the 40-kDa protein accepted either 6-aminopenicillanic acid or IPN as the substrate and made a penicillinase-sensitive antibiotic in the presence of phenylacetyl coenzyme A. Therefore, a single gene is responsible for converting IPN to penicillin G [10].
• Acyl coenzyme A: 6-aminopenicillanic acid acyltransferase from Penicillium chrysogenum and Aspergillus nidulans [11].

Chemical compound and disease context of Penicin

• Penicillin acylase formation by the hybrid strain Escherichia coli 5K(pHM12) was studied under different culture conditions and reached 200 to 250 mumol of 6-aminopenicillanic acid per min per g of bacteria (wet weight) for penicillin G [12].
• In vitro synthesis of penicillin G was achieved by incubating 6-aminopenicillanic acid, CoA, phenylacetic acid, homogeneously pure phenylacetyl-CoA ligase (PA-CoA ligase) from Pseudomonas putida and acyl-CoA:6-APA acyltransferase (AT) from Penicillium chrysogenum [13].

Biological context of Penicin

• A gene, aat, encoding acyl-CoA: 6-aminopenicillanic acid acyltransferase (AAT), the last enzyme of the penicillin (Pn) biosynthetic pathway, has been cloned from the genome of Penicillium chrysogenum AS-P-78 [14].
• Both substrates, ampicillin and 6-aminopenicillanic acid, protected the enzyme against inactivation, suggesting that the modification occurred near or at the active site [15].
• Random mutagenesis was conducted using a PAC-producing strain resistant to 6-aminopenicillanic acid (6-APA) as the parent strain and mutants were screened with penicillin at a high concentration [16].
• The intestinal absorption mechanisms of cefixime, 7-aminocephalosporanic acid (7-ACA) and 6-aminopenicillanic acid (6-APA) were determined from the results of single-pass perfusion experiments in rats by modified boundary layer analysis [17].
• The reactor equipped with either six or 12 pieces of cell-immobilized gluten membranes containing a biomass concentration of 5%, w/w was effective in catalyzing the production of 6-aminopenicillanic acid from penicillin G [18].

Associations of Penicin with other chemical compounds

• Equilibrium modeling of extractive enzymatic hydrolysis of penicillin G with concomitant 6-aminopenicillanic acid crystallization [19].
• Ionic strength and pH effects in the kinetically controlled synthesis of benzylpenicillin by nucleophilic deacylation of free and immobilized phenyl-acetyl-penicillin amidase with 6-aminopenicillanic acid [20].
• The penicillin acylase-catalyzed synthesis of ampicillin by acyl transfer from D-(-)-phenylglycine amide (D-PGA) to 6-aminopenicillanic acid (6-APA) becomes more effective when a judiciously chosen pH gradient is applied in the course of the process [21].
• Titration of 6-aminopenicillanic acid with mercury (II) solution [22].
• The beta-lactam compound 7-aminodesacetoxycephalosporanic acid (7-ADCA) was a better nucleophile than 6-aminopenicillanic acid, caused by a higher affinity of the enzyme for 7-ADCA and complete suppression of hydrolysis of the acyl-enzyme upon binding of 7-ADCA [23].

Gene context of Penicin

• Permeability of the outer membrane to 6-aminopenicillanic acid was unaltered in an lpo mutant, lacking the Braun lipoprotein, a result suggesting that the lipoproteins by themselves form no or few diffusion pores [24].
• Penicillin-binding protein 2 (PBP-2) of Escherichia coli K-12 was purified by covalent affinity chromatography using 6-aminopenicillanic acid covalently coupled to carboxymethyl-Sepharose (6-APA-CM-Sepharose) [25].
• Likewise the antibiotic derivatives 6-aminopenicillanic acid and 7-aminocephalosporanic acid are incorporated as carboxylate ligands. beta-Lactams bearing nitrophenyl or acyl substituents at the nitrogen atoms are opened hydrolytically by TpZn-OH, and the resulting N-substituted beta-amino acids are attached to zinc by their carboxylate functions [26].
• Forty-seven different penicillins, including some of great clinical importance, have been synthesized "in vitro" by coupling the newly described enzyme phenylacetyl-CoA ligase (PCL) from Pseudomonas putida and acyl-CoA: 6-aminopenicillanic acid (6-APA) acyltransferase (AT) from Penicillium chrysogenum [27].
• The introduction of 6-aminopenicillanate and 7-aminocephalosporanate to the C-3 side chain of carbapenem significantly reduced the antibacterial activity against the beta-lactamase-producing microbes [28].

Analytical, diagnostic and therapeutic context of Penicin

• We found that this conversion can exceed 90% because crystallization of 6-aminopenicillanic acid shifts the equilibrium to the product side [19].
• Inactivation by diazotized 6-aminopenicillanic acid was characterized further by tryptic and chymotryptic digestion of the inactivated enzyme and peptide mapping of the resulting digests [29].

References