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From Wikipedia, the free encyclopedia
In enzymology, a dihydroxyphenylalanine ammonia-lyase (EC 4.3.1.11, entry deleted) is a non-existing enzyme that catalyzes the chemical reaction
dihydroxyphenylalanine ammonia-lyase | |||||||||
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Identifiers | |||||||||
EC no. | 4.3.1.11 | ||||||||
CAS no. | 37290-92-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Hence, this enzyme has one substrate, 3,4-dihydroxy-L-phenylalanine (L-DOPA), 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.
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