32140-49-1Relevant articles and documents
Deracemization of racemic amino acids using (R)- and (S)-alanine racemase chiral analogues as chiral converters
Paik, Man-Jeong,Jeon, So Hee,Kang, Jong Seong,Kim, Kwan Mook,Lee, Wonjae
, p. 2186 - 2188 (2014/12/10)
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Fluorine Radiolabelling Process
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Paragraph 0521, (2013/07/31)
The invention relates to a process for producing a process for producing an 18F-labelled compound, the process comprising treating a compound of formula (I) wherein EDG is an electron-donating group selected from —OH, —OR4, —NHR5 and —NR55R5; R1, R2, X1 and X2 are as defined herein; and R3 is selected from H, X3 and X4, wherein X3 is a monodentate cleavable surrogate group, and X4 is a bidentate cleavable surrogate group which is bonded (a) to said X1 or X2 and (b) to the ring carbon atom para to EDG; with [18F]fluoride in the presence of an oxidant, thereby producing, when R3 in the compound of formula (I) is H, an 18F-labelled compound of formula (II), wherein EDG is as defined above and R1, R2, X1 and X2 are as defined herein; or thereby producing, when R3 in the compound of formula (I) is said monodentate cleavable surrogate group X3, a compound of formula (IIa), wherein EDG′ is O, NR5, —NR55R5 or [OR4]+, and wherein R4, R5, R55, R1, R2, X1, X2 and X3 are as defined herein; or thereby producing, when R3 in the compound of formula (I) is said bidentate cleavable surrogate group X4, a compound of formula (IIc) or a compound of formula (IId), wherein EDG′ is O, NR5, —NR55R5 or [OR4]+, and wherein R4, R5, R55, R1, R2, X1, X2 and X4 are as defined herein
Identification of phenylalanine 3-hydroxylase for meta -tyrosine biosynthesis
Zhang, Wenjun,Ames, Brian D.,Walsh, Christopher T.
scheme or table, p. 5401 - 5403 (2012/06/15)
Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (l-Phe) to l-tyrosine (l-Tyr). The enzymatic modification has been demonstrated to be highly regiospecific, forming proteinogenic para-Tyr (p-Tyr) exclusively. Here we biochemically characterized the first example of a phenylalanine 3-hydroxylase (Phe3H) that catalyzes the synthesis of meta-Tyr (m-Tyr) from Phe. Subsequent mutagenesis studies revealed that two residues in the active site of Phe3H (Cys187 and Thr202) contribute to C-3 rather than C-4 hydroxylation of the phenyl ring. This work sets the stage for the mechanistic and structural study of regiospecific control of the substrate hydroxylation by PheH.
