Question: What are large enzymes that make antibiotics called?
About the article "Evolution", section "Mutation".

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Encapsulins are a large and widely distributed family of proteins and are present in most bacteria and have been identified in "Candidatus methanoregula", a species of archaea.
They were originally called "linocin-like proteins" and thought to be a group of bacterial antibiotics, since they showed bacteriostatic activity in culture.
However, structural analysis showed these to form a spherical nanocompartment that contains enzymes involved in the defenses against oxidative stress. 
Like other beta-lactam antibiotics, meticillin acts by inhibiting the synthesis of bacterial cell walls.
It inhibits cross-linkage between the linear peptidoglycan polymer chains that make up a major component of the cell wall of Gram-positive bacteria.
It does this by binding to and competitively inhibiting the transpeptidase enzyme used by bacteria to cross-link the peptide ("D-alanyl-alanine") used in peptidoglycan synthesis.
Meticillin and other beta-lactam antibiotics are structural analogs of "D-alanyl-alanine", and the transpeptidase enzymes that bind to them are sometimes called penicillin-binding proteins (PBPs). 
New Delhi Metallo-beta-lactamase-1 (NDM-1) is an enzyme that makes bacteria resistant to a broad range of beta-lactam antibiotics.
These include the antibiotics of the carbapenem family, which are a mainstay for the treatment of antibiotic-resistant bacterial infections.
The gene for NDM-1 is one member of a large gene family that encodes beta-lactamase enzymes called carbapenemases.
Bacteria that produce carbapenemases are often referred to in the news media as "superbugs" because infections caused by them are difficult to treat.
Such bacteria are usually susceptible only to polymyxins and tigecycline.NDM-1 was first detected in a "Klebsiella pneumoniae" isolate from a Swedish patient of Indian origin in 2008.
It was later detected in bacteria in India, Pakistan, the United Kingdom, the United States, Canada, and Japan.
The most common bacteria that make this enzyme are Gram-negative such as "Escherichia coli" and "Klebsiella pneumoniae", but the gene for NDM-1 can spread from one strain of bacteria to another by horizontal gene transfer. 
Enzymes are large biological molecules responsible for the thousands of metabolic processes that sustain life.
They are highly selective catalysts, greatly accelerating both the rate and specificity of metabolic reactions, from the digestion of food to the synthesis of DNA.
Most enzymes are proteins, although some catalytic RNA molecules have been identified.
Enzymes adopt a specific three-dimensional structure, and may employ organic (e.g.
biotin) and inorganic (e.g.
magnesium ion) cofactors to assist in catalysis.
In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products.
Almost all chemical reactions in a biological cell need enzymes in order to occur at rates sufficient for life.
Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.
Like all catalysts, enzymes work by lowering the activation energy ("E"a‡) for a reaction, thus dramatically increasing the rate of the reaction.
As a result, products are formed faster and reactions reach their equilibrium state more rapidly.
Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions.
As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions.
However, enzymes do differ from most other catalysts in that they are highly specific for their substrates.
Enzymes are known to catalyze about 4,000 biochemical reactions.
A few RNA molecules called ribozymes also catalyze reactions, with an important example being some parts of the ribosome.
Synthetic molecules called artificial enzymes also display enzyme-like catalysis.
Enzyme activity can be affected by other molecules.
Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity.
Many drugs and poisons are enzyme inhibitors.
Activity is also affected by temperature, pressure, chemical environment (e.g., pH), and the concentration of substrate.
Some enzymes are used commercially, for example, in the synthesis of antibiotics.
In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins into smaller molecules, making the meat easier to chew). 
Resistance to beta-lactam antibiotics has become a particular problem in recent decades, as strains of bacteria that produce extended-spectrum beta-lactamases have become more common.
These beta-lactamase enzymes make many, if not all, of the penicillins and cephalosporins ineffective as therapy.
Extended-spectrum beta-lactamase–producing "E. coli" (ESBL "E. coli") are highly resistant to an array of antibiotics, and infections by these strains are difficult to treat.
In many instances, only two oral antibiotics and a very limited group of intravenous antibiotics remain effective.
In 2009, a gene called New Delhi metallo-beta-lactamase (shortened NDM-1) that even gives resistance to intravenous antibiotic carbapenem, were discovered in India and Pakistan on "E. coli" bacteria.
Increased concern about the prevalence of this form of "superbug" in the United Kingdom has led to calls for further monitoring and a UK-wide strategy to deal with infections and the deaths.
Susceptibility testing should guide treatment in all infections in which the organism can be isolated for culture.