Search results
Results from the WOW.Com Content Network
Aminoacylases have been used for the production of L-amino acids in industrial settings since the late 1950s. [18] Since aminoacylases are substrate specific for N-acyl-L-amino acids and not N-acyl-D-amino acids , aminoacylases can be used to reliably take a mixture of these two reactants and only convert the L enantiomers into products - which ...
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.
Medicinally, microbes can be used for creating antibiotics in order to treat infection. Microbes can also be used for the food industry as well. Microbes are very useful in creating some of the mass produced products that are consumed by people. The chemical industry also uses microorganisms in order to synthesize amino acids and organic solvents.
Industrial enzymes are enzymes that are commercially used in a variety of industries such as pharmaceuticals, chemical production, biofuels, food and beverage, and consumer products. Due to advancements in recent years, biocatalysis through isolated enzymes is considered more economical than use of whole cells.
In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic cofactors. [31] Enzyme structures may also contain allosteric sites where the binding of a small molecule causes a conformational change that increases or decreases activity.
Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is Sollpura (liprotamase), which help in the breakdown of saccharides into simple sugars.
The catalytic domain has a structure consisting of an eight-stranded α/β barrel that contains the active site, interrupted by a ~70-amino acid calcium-binding domain protruding between β-strand 3 and α-helix 3, and a carboxyl-terminal Greek key β-barrel domain. [23] Several α-amylases contain a β-sheet domain, usually at the C terminus.
These enzymes can be identified by a conserved HEXXH motif in their active site. This motif is crucial for the enzyme's function, as the histidine amino acids within the motif coordinate (bind) the metal ion, which then uses hydrolysis to break the peptide bond between the first amino acid and the rest of the protein. [9]