Dihydroxyphenylalanine ammonia-lyase
From Wikipedia, the free encyclopedia
In enzymology, a dihydroxyphenylalanine ammonia-lyase (EC 4.3.1.11) is an enzyme that catalyzes the chemical reaction
- 3,4-dihydroxy-L-phenylalanine trans-caffeate + NH3
Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine, and two products, trans-caffeate and NH3.
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.
[edit] References
- IUBMB entry for 4.3.1.11
- BRENDA references for 4.3.1.11 (Recommended.)
- PubMed references for 4.3.1.11
- PubMed Central references for 4.3.1.11
- Google Scholar references for 4.3.1.11
- MacLeod NJ and Pridham JB (1963). "Deamination of beta-(3,4-dihydroxyphenyl)-L-alanine by plants". Biochem. J. 88: 45.
[edit] External links
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- The CAS registry number for this enzyme class is 37290-92-9.