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  2. Tyrosine aminotransferase - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_aminotransferase

    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]

  3. Fumarylacetoacetate hydrolase - Wikipedia

    en.wikipedia.org/wiki/Fumarylacetoacetate_hydrolase

    Fumarylacetoacetate hydrolase (FAH) is a protein homodimer which cleaves fumarylacetoacetate at its carbon-carbon bond during a hydrolysis reaction. [8] As a critical enzyme in phenylalanine and tyrosine metabolism, 4-Fumarylacetoacetate hydrolase catalyzes the final step in the catabolism of 4-fumarylacetoacetate and water into acetoacetate, fumarate, and H + respectively. [9]

  4. Tyrosinemia type II - Wikipedia

    en.wikipedia.org/wiki/Tyrosinemia_type_II

    Type II tyrosinemia is caused by a deficiency of the enzyme tyrosine aminotransferase (EC 2.6.1.5), encoded by the gene TAT.Tyrosine aminotransferase is the first in a series of five enzymes that converts tyrosine to smaller molecules, which are excreted by the kidneys or used in reactions that produce energy.

  5. Tyrosinemia - Wikipedia

    en.wikipedia.org/wiki/Tyrosinemia

    All tyrosinemias result from dysfunction of various genes in the phenylalanine and tyrosine catabolic pathway, and are inherited in an autosomal-recessive pattern. [ 3 ] Type I tyrosinemia results from a mutation in the FAH gene, which encodes the enzyme fumarylacetoacetase. [ 4 ]

  6. Xanthoproteic reaction - Wikipedia

    en.wikipedia.org/wiki/Xanthoproteic_reaction

    The xanthoproteic reaction is a method that can be used to detect a presence of protein soluble in a solution, using concentrated nitric acid. The test gives a positive result in amino acids carrying aromatic groups, especially in the presence of tyrosine. If the test is positive the proof is neutralized with an alkali, turning dark yellow.

  7. Tyrosinase - Wikipedia

    en.wikipedia.org/wiki/Tyrosinase

    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 ...

  8. 4-Hydroxyphenylpyruvate dioxygenase - Wikipedia

    en.wikipedia.org/wiki/4-Hydroxyphenylpyruvate_di...

    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).

  9. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature.