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The enzyme tyrosine phenol-lyase (EC 4.1.99.2) catalyzes the chemical reaction L -tyrosine + H 2 O ⇌ {\displaystyle \rightleftharpoons } 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]
Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase.
The shikimate pathway (shikimic acid pathway) is a seven-step metabolic pathway used by bacteria, archaea, fungi, algae, some protozoans, and plants for the biosynthesis of folates and aromatic amino acids (tryptophan, phenylalanine, and tyrosine). This pathway is not found in mammals.
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 ...
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 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]
HPPD is an enzyme that usually bonds to form tetramers in bacteria and dimers in eukaryotes and has a subunit mass of 40-50 kDa. [7] [8] [9] Dividing the enzyme into the N-terminus and C-terminus one will notice that the N-terminus varies in composition while the C-terminus remains relatively constant [10] (the C-terminus in plants does differ slightly from the C-terminus in other beings).