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The enzyme tyrosine phenol-lyase (EC 4.1.99.2) catalyzes the chemical reaction. L-tyrosine + H 2 O phenol + pyruvate + NH 3. This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases.
Tyrosine ammonia lyase (TAL) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid. Tyrosine is also the precursor to the pigment melanin. Tyrosine (or its precursor phenylalanine) is needed to synthesize the benzoquinone structure which forms part of coenzyme Q10. [23] [24]
This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
22173 Ensembl ENSG00000077498 ENSMUSG00000004651 UniProt P14679 P11344 RefSeq (mRNA) NM_000372 NM_011661 NM_001317397 RefSeq (protein) NP_000363 NP_001304326 NP_035791 Location (UCSC) Chr 11: 89.18 – 89.3 Mb Chr 7: 87.07 – 87.14 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tyrosinase is an oxidase that is the rate-limiting enzyme for controlling the production of melanin. The ...
Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine ...
The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.: [1] L -phenylalanine = trans -cinnamate + NH 3 Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol ...
In plants, all phenylpropanoids are derived from the amino acids phenylalanine and tyrosine. Phenylalanine ammonia-lyase (PAL, a.k.a. phenylalanine/tyrosine ammonia-lyase) is an enzyme that transforms L-phenylalanine and tyrosine into trans-cinnamic acid and p-coumaric acid, respectively.
In humans, the tyrosine aminotransferase protein is encoded by the TAT gene. [7] A deficiency of the enzyme in humans can result in what is known as type II tyrosinemia, wherein there is an abundance of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction to form 4-hydroxyphenylpyruvate. [8]