Penicillin Amidase
Penicillins
Amidohydrolases
Enzymes, Immobilized
Penicillin G
Penicillin V
N-Acetylmuramoyl-L-alanine Amidase
Substrate Specificity
Escherichia coli
In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130. (1/125)
Cephalosporin acylases are a group of enzymes that hydrolyze cephalosporin C (CPC) and/or glutaryl 7-amino cephalosporanic acid (GL-7ACA) to produce 7-amino cephalosporanic acid (7-ACA). The acylase from Pseudomonas sp. 130 (CA-130) is highly active on GL-7ACA and glutaryl 7-aminodesacetoxycephalosporanic acid (GL-7ADCA), but much less active on CPC and penicillin G. The gene encoding the enzyme is expressed as a precursor polypeptide consisting of a signal peptide followed by alpha- and beta-subunits, which are separated by a spacer peptide. Removing the signal peptide has little effect on precursor processing or enzyme activity. Substitution of the first residue of the beta-subunit, Ser, results in a complete loss of enzyme activity, and substitution of the last residue of the spacer, Gly, leads to an inactive and unprocessed precursor. The precursor is supposed to be processed autocatalytically, probably intramolecularly. The two subunits of the acylase, which separately are inactive, can generate enzyme activity when coexpressed in Escherichia coli. Data on this and other related acylases indicate that the cephalosporin acylases may belong to a novel class of enzymes (N-terminal nucleophile hydrolases) described recently. (+info)Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli. (2/125)
The penicillin amidase (PA) from Escherichia coli belongs to a group of proteolytically processed bacterial enzymes. The mechanism of the maturation of the single polypeptide proenzyme has been studied for the PA from E. coli using a slowly processing mutant proenzyme. The mutant proenzyme was constructed by replacing Thr with Gly in the Thr(263)-Ser(264) bond that must be hydrolysed in active PA. The mutant proenzyme was purified by biospecific affinity chromatography using an immobilized monoclonal antibody against PA. The maturation of the free and covalently immobilized purified proenzyme was studied in vitro. For the free proenzyme the same products with PA activity as observed in homogenates of wild-type PA-producing E. coli cells were found to be formed during this process. A kinetic analysis of the possible inter- and intramolecular processes involved in the maturation demonstrated that unambiguous evidence for the existence of intramolecular processes can only be obtained in systems where intermolecular processes are excluded. The Gly(263)-Ser(264) bond was found to be hydrolysed first in the free and immobilized mutant proenzyme, based on determinations of mass spectra, N-terminal sequences and active site concentrations. In the system with immobilized proenzyme intermolecular processes are excluded, demonstrating that this bond is hydrolysed by intramolecular autoproteolysis. Based on the known three-dimensional structure of the PA from E. coli the same maturation mechanism should apply for the wild-type proenzyme. (+info)pH dependence of penicillin amidase enantioselectivity for charged substrates. (3/125)
The pH dependence of E (enantiomeric ratio or enantioselectivity, a quantitative measure for enzyme stereospecificity) was studied for penicillin amidase catalysed hydrolysis of charged enantiomeric substrates. Theoretical analysis shows that a pH dependence can only be observed around the pK values of groups in the active site whose ionisation control the enzyme activity. For charged substrates that may perturb these pK values, a pH dependence of E is also expected. This was experimentally verified around these pK values. The S'(1)-stereospecificity of penicillin amidase was studied for the hydrolysis of the enantiomeric phenylacetyl-S/R-Phe and for the racemic phenylacetyl-S,R-PhG. The S(1)-stereospecificity was investigated for the hydrolysis of the enantiomeric S/R-PhG-NH(2). The observed pH modulation of E (more than 3-fold for the studied substrates in the pH range 4.5-9) was found to be a result of compensatory effects for binding and catalysis. The ratios k(cat, S)/k(cat,R) and K(m,S)/K(m,R) for the hydrolysis of the enantiomeric phenylacetyl-Phe were found to decrease from 1000 to 10 and from 0.1 to 0.01, respectively in the pH range 5-8. The dependence was stronger for the S'(1)- than for the S(1)-subsite. This is probably due to the stronger influence of the substrate carboxyl group in the S'(1)-subsite than that of the substrate amino group in the S(1)-subsite on the pK of the N-terminal Ser B1 that is essential for the activity. The observed pH dependence of E was used to discuss the importance of ground-state interactions for discrimination between enantiomers and for enzyme catalysis in general. The experimental results conform to the split site model according to which a better binding must not be fundamentally inhibitory. (+info)Enzymatic synthesis of beta-lactam antibiotics using penicillin-G acylase in frozen media. (4/125)
Penicillin-G acylase (EC 3.5.1.11) from Escherichia coli catalyzed the synthesis of various beta-lactam antibiotics in ice at -20 degrees C with higher yields than obtained in solution at 20 degrees C. The initial ratio between aminolysis and hydrolysis of the acyl-enzyme complex in the synthesis of cephalexin increased from 1.3 at 20 degrees C to 25 at -20 degrees C. The effect on the other antibiotics studied was less, leading us to conclude that freezing of the reaction medium influences the hydrolysis of each nucleophile-acyl-enzyme complex to a different extent. Only free penicillin-G acylase could perform transformations in frozen media: immobilized preparations showed a low, predominantly hydrolytic activity under these conditions. (+info)Processing and functional display of the 86 kDa heterodimeric penicillin G acylase on the surface of phage fd. (5/125)
The large heterodimeric penicillin G acylase from Alcaligenes faecalis was displayed on the surface of phage fd. We fused the coding sequence (alpha subunit-internal peptide-beta subunit) to the gene of a phage coat protein. A modified g3p signal sequence was used to direct the polypeptide to the periplasm. Here we show that a heterodimeric enzyme can be expressed as a fusion protein that matures to an active biocatalyst connected to the coat protein of phage fd, resulting in a phage to which the beta-subunit is covalently linked and the alpha-subunit is non-covalently attached. The enzyme can be displayed either fused to the minor coat protein g3p or fused to the major coat protein g8p. In both cases the penicillin G acylase on the phage has the same Michaelis constant as its freely soluble counterpart, indicating a proper folding and catalytic activity of the displayed enzyme. The display of the heterodimer on phage not only allows its further use in protein engineering but also offers the possibility of applying this technology for the excretion of the enzyme into the extracellular medium, facilitating purification of the protein. With the example of penicillin acylase the upper limit for a protein to become functionally displayed by phage fd has been further explored. Polyvalent display was not observed despite the use of genetic constructs designed for this aim. These results are discussed in relation to the pore size being formed by the g4p multimer. (+info)Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri. (6/125)
Penicillin G acylase is an important enzyme in the commercial production of semisynthetic penicillins used to combat bacterial infections. Mutant strains of Providencia rettgeri were generated from wild-type cultures subjected to nutritional selective pressure. One such mutant, Bro1, was able to use 6-bromohexanamide as its sole nitrogen source. Penicillin acylase from the Bro1 strain exhibited an altered substrate specificity consistent with the ability of the mutant to process 6-bromohexanamide. The X-ray structure determination of this enzyme was undertaken to understand its altered specificity and to help in the design of site-directed mutants with desired specificities. In this paper, the structure of the Bro1 penicillin G acylase has been solved at 2.5 A resolution by molecular replacement. The R-factor after refinement is 0.154 and R-free is 0.165. Of the 758 residues in the Bro1 penicillin acylase heterodimer (alpha-subunit, 205; beta-subunit, 553), all but the eight C-terminal residues of the alpha-subunit have been modeled based on a partial Bro1 sequence and the complete wild-type P. rettgeri sequence. A tightly bound calcium ion coordinated by one residue from the alpha-subunit and five residues from the beta-subunit has been identified. This enzyme belongs to the superfamily of Ntn hydrolases and uses Ogamma of Ser beta1 as the characteristic N-terminal nucleophile. A mutation of the wild-type Met alpha140 to Leu in the Bro1 acylase hydrophobic specificity pocket is evident from the electron density and is consistent with the observed specificity change for Bro1 acylase. The electron density for the N-terminal Gln of the alpha-subunit is best modeled by the cyclized pyroglutamate form. Examination of aligned penicillin acylase and cephalosporin acylase primary sequences, in conjunction with the P. rettgeri and Escherichia coli penicillin acylase crystal structures, suggests several mutations that could potentially allow penicillin acylase to accept charged beta-lactam R-groups and to function as a cephalosporin acylase and thus be used in the manufacture of semi-synthetic cephalosporins. (+info)The role of alpha-amino group of the N-terminal serine of beta subunit for enzyme catalysis and autoproteolytic activation of glutaryl 7-aminocephalosporanic acid acylase. (7/125)
Glutaryl 7-aminocephalosporanic acid (GL-7-ACA) acylase of Pseudomonas sp. strain GK16 catalyzes the cleavage of the amide bond in the GL-7-ACA side chain to produce glutaric acid and 7-aminocephalosporanic acid (7-ACA). The active enzyme is an (alphabeta)(2) heterotetramer of two non-identical subunits that are cleaved autoproteolytically from an enzymatically inactive precursor polypeptide. In this study, we prepared and characterized a chemically modified enzyme, and also examined an effect of the modification on enzyme catalysis and autocatalytic processing of the enzyme precursor. We found that treatment of the enzyme with cyanate ion led to a significant loss of the enzyme activity. Structural and functional analyses of the modified enzyme showed that carbamylation of the free alpha-amino group of the N-terminal Ser-199 of the beta subunit resulted in the loss of the enzyme activity. The pH dependence of the kinetic parameters indicates that a single ionizing group is involved in enzyme catalysis with pK(a) = 6.0, which could be attributed to the alpha-amino group of the N-terminal Ser-199. The carbamylation also inhibited the secondary processing of the enzyme precursor, suggesting a possible role of the alpha-amino group for the reaction. Mutagenesis of the invariant N-terminal residue Ser-199 confirmed the key function of its side chain hydroxyl group in both enzyme catalysis and autoproteolytic activation. Partial activity and correct processing of a mutant S199T were in agreement with the general mechanism of N-terminal nucleophile hydrolases. Our results indicate that GL-7-ACA acylase utilizes as a nucleophile Ser-199 in both enzyme activity and autocatalytic processing and most importantly its own alpha-amino group of the Ser-199 as a general base catalyst for the activation of the hydroxyl group both in enzyme catalysis and in the secondary cleavage of the enzyme precursor. All of the data also imply that GL-7-ACA acylase is a member of a novel class of N-terminal nucleophile hydrolases that have a single catalytic center for enzyme catalysis. (+info)The 2.0 A crystal structure of cephalosporin acylase. (8/125)
BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is usually obtained by chemical deacylation of cephalosporin C (CPC). The chemical production of 7-ACA includes, however, several expensive steps and requires thorough treatment of chemical wastes. Therefore, an enzymatic conversion of CPC to 7-ACA by cephalosporin acylase is of great interest. The biggest obstacle preventing this in industrial production is that cephalosporin acylase uses glutaryl-7ACA as a primary substrate and has low substrate specificity for CPC. RESULTS: We have solved the first crystal structure of a cephalosporin acylase from Pseudomonas diminuta at 2.0 A resolution. The overall structure looks like a bowl with two "knobs" consisting of helix- and strand-rich regions, respectively. The active site is mostly formed by the distinctive structural motif of the N-terminal (Ntn) hydrolase superfamily. Superposition of the 61 residue active-site pocket onto that of penicillin G acylase shows an rmsd in Calpha positions of 1.38 A. This indicates structural similarity in the active site between these two enzymes, but their overall structures are elsewhere quite different. CONCLUSION: The substrate binding pocket of the P. diminuta cephalosporin acylase provides detailed insight into the ten key residues responsible for the specificity of the cephalosporin C side chain in four classes of cephalosporin acylases, and it thereby forms a basis for the design of an enzyme with an improved conversion rate of CPC to 7-ACA. The structure also provides structural evidence that four of the five different classes of cephalosporin acylases can be grouped into one family of the Ntn hydrolase superfamily. (+info)Penicillin amidase is not a medical term per se, but rather a biochemical term. It's also known as penicillin acylase or simply penicillinase. It refers to an enzyme that can break down certain types of penicillin antibiotics by cleaving the amide bond in the beta-lactam ring, which is the core structure of these antibiotics. This makes the antibiotic ineffective.
Beta-lactam antibiotics include penicillins and cephalosporins, among others. Some bacteria produce penicillin amidases as a form of resistance to these antibiotics. The enzyme can be used in biotechnology to produce semi-synthetic penicillins by cleaving the side chain of a parent penicillin and then attaching a different side chain, creating a new antibiotic with potentially different properties.
Penicillins are a group of antibiotics derived from the Penicillium fungus. They are widely used to treat various bacterial infections due to their bactericidal activity, which means they kill bacteria by interfering with the synthesis of their cell walls. The first penicillin, benzylpenicillin (also known as penicillin G), was discovered in 1928 by Sir Alexander Fleming. Since then, numerous semi-synthetic penicillins have been developed to expand the spectrum of activity and stability against bacterial enzymes that can inactivate these drugs.
Penicillins are classified into several groups based on their chemical structure and spectrum of activity:
1. Natural Penicillins (e.g., benzylpenicillin, phenoxymethylpenicillin): These have a narrow spectrum of activity, mainly targeting Gram-positive bacteria such as streptococci and staphylococci. However, they are susceptible to degradation by beta-lactamase enzymes produced by some bacteria.
2. Penicillinase-resistant Penicillins (e.g., methicillin, oxacillin, nafcillin): These penicillins resist degradation by certain bacterial beta-lactamases and are primarily used to treat infections caused by staphylococci, including methicillin-susceptible Staphylococcus aureus (MSSA).
3. Aminopenicillins (e.g., ampicillin, amoxicillin): These penicillins have an extended spectrum of activity compared to natural penicillins, including some Gram-negative bacteria such as Escherichia coli and Haemophilus influenzae. However, they are still susceptible to degradation by many beta-lactamases.
4. Antipseudomonal Penicillins (e.g., carbenicillin, ticarcillin): These penicillins have activity against Pseudomonas aeruginosa and other Gram-negative bacteria with increased resistance to other antibiotics. They are often combined with beta-lactamase inhibitors such as clavulanate or tazobactam to protect them from degradation.
5. Extended-spectrum Penicillins (e.g., piperacillin): These penicillins have a broad spectrum of activity, including many Gram-positive and Gram-negative bacteria. They are often combined with beta-lactamase inhibitors to protect them from degradation.
Penicillins are generally well-tolerated antibiotics; however, they can cause allergic reactions in some individuals, ranging from mild skin rashes to life-threatening anaphylaxis. Cross-reactivity between different penicillin classes and other beta-lactam antibiotics (e.g., cephalosporins) is possible but varies depending on the specific drugs involved.
Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).
The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.
Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.
Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.
Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.
Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.
Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.
Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.
Penicillin G is a type of antibiotic that belongs to the class of medications called penicillins. It is a natural antibiotic derived from the Penicillium fungus and is commonly used to treat a variety of bacterial infections. Penicillin G is active against many gram-positive bacteria, as well as some gram-negative bacteria.
Penicillin G is available in various forms, including an injectable solution and a powder for reconstitution into a solution. It works by interfering with the ability of bacteria to form a cell wall, which ultimately leads to bacterial death. Penicillin G is often used to treat serious infections that cannot be treated with other antibiotics, such as endocarditis (inflammation of the inner lining of the heart), pneumonia, and meningitis (inflammation of the membranes surrounding the brain and spinal cord).
It's important to note that Penicillin G is not commonly used for topical or oral treatment due to its poor absorption in the gastrointestinal tract and instability in acidic environments. Additionally, as with all antibiotics, Penicillin G should be used under the guidance of a healthcare professional to ensure appropriate use and to reduce the risk of antibiotic resistance.
Penicillin V, also known as Penicillin V Potassium, is an antibiotic medication used to treat various bacterial infections. It belongs to the class of medications called penicillins, which work by interfering with the bacteria's ability to form a protective covering (cell wall), causing the bacteria to become more susceptible to destruction by the body's immune system.
Penicillin V is specifically used to treat infections of the respiratory tract, skin, and ear. It is also used to prevent recurrent rheumatic fever and chorea (Sydenham's chorea), a neurological disorder associated with rheumatic fever.
The medication is available as oral tablets or liquid solutions and is typically taken by mouth every 6 to 12 hours, depending on the severity and type of infection being treated. As with any antibiotic, it is important to take Penicillin V exactly as directed by a healthcare professional and for the full duration of treatment, even if symptoms improve before all doses have been taken.
Penicillin V is generally well-tolerated, but like other penicillins, it can cause allergic reactions in some people. It may also interact with certain medications, so it is important to inform a healthcare provider of any other medications being taken before starting Penicillin V therapy.
Penicillin resistance is the ability of certain bacteria to withstand the antibacterial effects of penicillin, a type of antibiotic. This occurs when these bacteria have developed mechanisms that prevent penicillin from binding to and inhibiting the function of their cell wall biosynthesis proteins, particularly the enzyme transpeptidase.
One common mechanism of penicillin resistance is the production of beta-lactamases, enzymes that can hydrolyze and inactivate the beta-lactam ring structure present in penicillin and other related antibiotics. Another mechanism involves alterations in the bacterial cell wall that prevent penicillin from binding to its target proteins.
Penicillin resistance is a significant concern in clinical settings, as it can limit treatment options for bacterial infections and may necessitate the use of more potent or toxic antibiotics. It is important to note that misuse or overuse of antibiotics can contribute to the development and spread of antibiotic-resistant bacteria, including those resistant to penicillin.
N-Acetylmuramoyl-L-alanine Amidase (also known as NAM Amidase or MurNAc-LAA Amidase) is an enzyme that plays a crucial role in the bacterial cell wall metabolism. It is responsible for cleaving the amide bond between N-acetylmuramic acid (NAM) and L-alanine (L-Ala) in the peptidoglycan, which is a major component of the bacterial cell wall.
The enzyme's systematic name is N-acetylmuramoyl-L-alanine amidase, but it can also be referred to as:
* N-acetylmuramic acid lyase
* Peptidoglycan N-acetylmuramoylhydrolase
* N-acetylmuramoyl-L-alanine glycohydrolase
* N-acetylmuramoyl-L-alanine amidohydrolase
N-Acetylmuramoyl-L-alanine Amidase is an essential enzyme for bacterial cell division and morphogenesis, as it facilitates the separation of daughter cells by cleaving peptidoglycan crosslinks. This enzyme has been studied extensively due to its potential as a target for developing new antibiotics that can selectively inhibit bacterial cell wall biosynthesis without affecting human cells.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
Penicillin G Procaine is a formulation of penicillin G, an antibiotic derived from the Penicillium fungus, combined with procaine, a local anesthetic. This combination is often used for its extended-release properties and is administered intramuscularly. It is primarily used to treat moderate infections caused by susceptible strains of streptococci and staphylococci.
The procaine component helps to reduce the pain at the injection site, while penicillin G provides the antibacterial action. The extended-release formulation allows for less frequent dosing compared to immediate-release penicillin G. However, its use has become less common due to the development of other antibiotics and routes of administration.
Penicillin G Benzathine is a type of antibiotic that is used to treat various bacterial infections. According to the International Journal of Antimicrobial Agents, Penicillin G Benzathine is a "water-soluble salt of penicillin G, which has a very high degree of stability and provides prolonged low-level serum concentrations after intramuscular injection."
It is often used to treat infections caused by streptococci and treponema pallidum, the bacterium that causes syphilis. Penicillin G Benzathine works by interfering with the ability of these bacteria to form a cell wall, which is essential for their survival. Without a functional cell wall, the bacteria are unable to grow and multiply, and are eventually destroyed by the body's immune system.
Penicillin G Benzathine is typically administered via intramuscular injection, and its prolonged release allows for less frequent dosing compared to other forms of penicillin. However, it may not be suitable for all patients, particularly those with a history of allergic reactions to penicillin or other antibiotics. As with any medication, Penicillin G Benzathine should only be used under the supervision of a healthcare provider.
Penicillin amidase
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Acylase3
- Penicillin acylase of Escherichia coli catalyses the hydrolysis and synthesis of beta-lactam antibiotics. (hanze.nl)
- A novel approach for the isolation and purification of penicillin acylase (PA), which couples aqueous two-phase partitioning and enzyme immobilization has been investigated. (aber.ac.uk)
- Guan, Y, Brook, AH & Lilley, TH 2001, ' Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization ', Enzyme and Microbial Technology , vol. 28, no. 2-3, pp. 2-3. (aber.ac.uk)
Peptidoglycan2
- Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli . (bio-protocol.org)
- Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli . (bio-protocol.org)
Enzyme6
- In enzymology, a penicillin amidase (EC 3.5.1.11) is an enzyme that catalyzes the chemical reaction penicillin + H2O ⇌ {\displaystyle \rightleftharpoons } a carboxylate + 6-aminopenicillanate Thus, the two substrates of this enzyme are penicillin and H2O, whereas its two products are carboxylate and 6-aminopenicillanate. (wikipedia.org)
- The systematic name of this enzyme class is penicillin amidohydrolase. (wikipedia.org)
- This enzyme participates in penicillin and cephalosporin biosynthesis. (wikipedia.org)
- An enzyme catalyzing the hydrolysis of penicillin to penicin and a carboxylic acid anion. (musc.edu)
- FBL is a pioneer in the development and production of fermentation-based Penicillin G Amidase enzyme (PGA) and commercialized immobilized enzymes in India. (assianews.com)
- An in situ enzyme immobilization approach, using oxirane acrylic or aldehyde-agarose beads dispersed in the PEG-rich phase, was explored for the conversion of penicillin G to 6-aminopenicillanic acid. (aber.ac.uk)
Escherichia3
- Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching. (bio-protocol.org)
- Loss of O-antigen increases cell shape abnormalities in penicillin-binding protein mutants of Escherichia coli . (bio-protocol.org)
- Gentamicin belongs to aminoglycoside antibiotics, which has antibacterial effect on a variety of gram-negative bacteria (such as Escherichia coli, Klebsiella, Proteus, pseudomonas aeruginosa, Pasteurella, Salmonella, etc.) and Staphylococcus aureus (including β -amidase producing strains). (veterinarymedicinedrugs.com)
Semisynthetic1
- A low amidase activity was also observed for the semisynthetic penicillins amoxicillin and ampicillin and the cephalosporins cefadroxil and cephalexin, for which the kcat values were fivefold to 10-fold lower than the wild-type values. (hanze.nl)
Outer membrane1
- Salvage of polymeric PGN presumably requires the removal of peptides from PGN by an unknown amidase, concomitantly with the translocation of the polymer across the outer membrane. (karger.com)
Derivative1
- A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. (definitions.net)
Benzylpenicillin3
- Benzylpenicillin, also known as penicillin G (PenG) or BENPEN, and in US military slang "Peanut Butter Shot" is an antibiotic used to treat a number of bacterial infections. (definitions.net)
- Use during pregnancy is generally safe in the penicillin and β-lactam class of medications.Benzylpenicillin is on the World Health Organization's List of Essential Medicines. (definitions.net)
- Penicillin G, also known as Benzylpenicillin, is a naturally occurring antibiotic derived from the Penicillium fungi. (definitions.net)
Antibiotics1
- The use of a variety of manufacturing methods for the composite, such as food and medicines, such as antibiotics, such as penicillin and artificial enzymes. (candle4tibet.org)
Production3
- As the full burden of parents induced significantly higher amount of structure amidase Ajay - G - cell design, the production of penicillin, thanks to the plasmid amplification at around 50 copies per cell. (candle4tibet.org)
- 2018. Generic flowsheeting approach to generating first estimate material and energy balance data for Life Cycle Assessment (LCA) of Penicillin V production. (uct.ac.za)
- Improving the production of a thermostable amidase through optimising IPTG induction in a highly dense culture of recombinant E.coli. (uct.ac.za)
Consumption1
- Penicillin G can be administered through oral consumption or intravenous injection, depending on the severity of the infection. (definitions.net)
General1
- Accidental death often occurs in dogs and cats under surgical general anaesthesia when combined with penicillin to prevent infection. (veterinarymedicinedrugs.com)
Total1
- This graph shows the total number of publications written about "Penicillin Amidase" by people in this website by year, and whether "Penicillin Amidase" was a major or minor topic of these publications. (musc.edu)
Amidohydrolase1
- The systematic name of this enzyme class is penicillin amidohydrolase. (wikipedia.org)
1.111
- In enzymology, a penicillin amidase (EC 3.5.1.11) is an enzyme that catalyzes the chemical reaction penicillin + H2O ⇌ {\displaystyle \rightleftharpoons } a carboxylate + 6-aminopenicillanate Thus, the two substrates of this enzyme are penicillin and H2O, whereas its two products are carboxylate and 6-aminopenicillanate. (wikipedia.org)
CEPHALOSPORINS4
- Bacterial resistance to penicillins and cephalosporins. (nih.gov)
- High concentrations of penicillin G, other penicillins or cephalosporins were necessary for optimal induction. (microbiologyresearch.org)
- The structure of both the nucleus and side chain of the penicillins and cephalosporins determined the rate of their hydrolysis by the β-lactamase. (microbiologyresearch.org)
- These results indicate that the resistance of the bacteria to the β-lactamase-sensitive penicillins and to cephalosporins is dependent on a combined effect of β-lactamase and on an intrinsic resistance, while the resistance of the bacteria to the β-lactamase-resistant penicillins depends on the intrinsic resistance alone. (microbiologyresearch.org)
BACTERIA1
- The role of penicillinase in determining natural and acquired resistance of Gram-negative bacteria to penicillins. (microbiologyresearch.org)
Chemistry1
- Manufacturing fermentation based pharma products like erythromycin and penicillin, R&D in chemistry, microbiology and pharmaceutical technonolgy and bioequivalence. (indiabiotech.in)
Reaction1
- Manometric method of assaying penicillinase and penicillin, kinetics of the penicillin-penicillinase reaction, and the effects of inhibitors on penicillinase. (microbiologyresearch.org)
Rabbit1
- 7. An amidase of rabbit liver. (qmul.ac.uk)
Streptomycin1
- Cell Culture The IPEC-J2 cells were preserved in our laboratory, and cultured in Dulbeccos altered Eagles medium (DMEM) made up of 10% fetal bovine serum (FBS) and 1% penicillin streptomycin (1 mg/mL) at 37C with 5% CO2. (bioinf.org)
Organic1
- Products to pharmaceutical companies are fermentation based penicillin G, custom synthesis and contract manufacturing of active pharmaceutical ingredients, synthetic organic compounds, drug intermediates and plant based nutraceuticals. (indiabiotech.in)