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Dihydroxyphenylalanine ammonia-lyase
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In enzymology, a dihydroxyphenylalanine ammonia-lyase (, entry deleted) is a non-existing enzyme that catalyzes the chemical reaction :3,4-dihydroxy-L-phenylalanine <math>\rightleftharpoons</math> trans-caffeate + NH<sub>3</sub> Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine (L-DOPA), and two products, trans-caffeate and NH<sub>3</sub>. This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 3,4-dihydroxy-L-phenylalanine ammonia-lyase (trans-caffeate-forming). Other names in common use include beta-(3,4-dihydroxyphenyl)-L-alanine (DOPA) ammonia-lyase, and 3,4-dihydroxy-L-phenylalanine ammonia-lyase. This enzyme participates in tyrosine metabolism. |
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