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Tyrosine 2,3-aminomutase
・ Tyrosine aminotransferase
・ Tyrosine ammonia-lyase
・ Tyrosine decarboxylase
・ Tyrosine hydroxylase
・ Tyrosine kinase
・ Tyrosine kinase 2
・ Tyrosine N-monooxygenase
・ Tyrosine phenol-lyase
・ Tyrosine phosphorylation
・ Tyrosine sulfation
・ Tyrosine-ester sulfotransferase
・ Tyrosine-kinase inhibitor
・ Tyrosine-protein kinase BLK
・ Tyrosine-protein kinase CSK


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Tyrosine 2,3-aminomutase : ウィキペディア英語版
Tyrosine 2,3-aminomutase

In enzymology, a tyrosine 2,3-aminomutase () is an enzyme that catalyzes the chemical reaction
:L-tyrosine \rightleftharpoons 3-amino-3-(4-hydroxyphenyl)propanoate
Hence, this enzyme has one substrate, L-tyrosine, and one product, 3-amino-3-(4-hydroxyphenyl)propanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is L-tyrosine 2,3-aminomutase. This enzyme is also called tyrosine alpha,beta-mutase. This enzyme participates in tyrosine metabolism. It employs one cofactor, 5-methylene-3,5-dihydroimidazol-4-one (MIO) which is formed autocatalytic rearrangement of the internal tripeptide Ala-Ser-Gly.
==Structural studies==

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .

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