Dihydroxyphenylalanine ammonia-lyase
Dihydroxyphenylalanine ammonia-lyase[edit | edit source]
The structure of Dihydroxyphenylalanine ammonia-lyase.
Dihydroxyphenylalanine ammonia-lyase (DOPAL) is an enzyme that plays a crucial role in the biosynthesis of various important compounds in living organisms. It is also known as phenylalanine ammonia-lyase (PAL) or L-phenylalanine ammonia-lyase.
Function[edit | edit source]
Dihydroxyphenylalanine ammonia-lyase catalyzes the deamination of L-phenylalanine to trans-cinnamic acid and ammonia. This reaction is an important step in the phenylpropanoid pathway, which is responsible for the production of a wide range of secondary metabolites, including flavonoids, lignins, and coumarins. These compounds have various biological functions, such as defense against pathogens and UV radiation, as well as roles in plant growth and development.
Structure[edit | edit source]
DOPAL is a homotetrameric enzyme, meaning it consists of four identical subunits. Each subunit contains a catalytic domain responsible for the enzymatic activity and a regulatory domain that controls the enzyme's function. The catalytic domain contains a conserved active site where the deamination of L-phenylalanine takes place.
Role in Disease[edit | edit source]
Mutations in the gene encoding DOPAL have been associated with various diseases in humans. For example, deficiencies in DOPAL activity have been linked to phenylketonuria (PKU), a metabolic disorder characterized by the accumulation of phenylalanine in the blood. PKU can lead to intellectual disability and other neurological problems if left untreated.
Applications[edit | edit source]
DOPAL has gained significant attention in the field of biotechnology due to its potential applications. The enzyme can be used in the production of trans-cinnamic acid, which has various industrial uses, including the synthesis of fragrances, flavors, and pharmaceuticals. Additionally, DOPAL has been explored for its potential in the production of biofuels and as a biocatalyst in organic synthesis.
References[edit | edit source]
See Also[edit | edit source]
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