Tyrosine, 3-fluoro-
Tyrosine, 3-fluoro- structure
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Common Name | Tyrosine, 3-fluoro- | ||
|---|---|---|---|---|
| CAS Number | 403-90-7 | Molecular Weight | 199.17900 | |
| Density | 1.421g/cm3 | Boiling Point | 362.4ºC at 760mmHg | |
| Molecular Formula | C9H10FNO3 | Melting Point | 276-280ºC | |
| MSDS | Chinese USA | Flash Point | 172.9ºC | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase.
Biochemistry 45(31) , 9575-83, (2006) Tyrosine phenol-lyase (TPL) from Citrobacter freundii is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible hydrolytic cleavage of l-Tyr to give phenol and ammonium pyruvate. The proposed reaction mechanism for TPL involves formatio... |
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Hydrogen bonding in human manganese superoxide dismutase containing 3-fluorotyrosine.
Biophys. J. 89(6) , 4171-9, (2005) Incorporation of 3-fluorotyrosine and site-specific mutagenesis has been utilized with Fourier transform infrared (FTIR) spectroscopy and x-ray crystallography to elucidate active-site structure and the role of an active-site residue Tyr34 in human manganese ... |
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Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine.
J. Mol. Biol. 281(2) , 323-39, (1998) The structure of the tetradeca-(3-fluorotyrosyl) M1-1 GSH transferase (3-FTyr GSH transferase), a protein in which tyrosine residues are globally substituted by 3-fluorotyrosines has been determined at 2.2 A resolution. This variant was produced to study the ... |
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6-[18F]fluoro-L-m-tyrosine: metabolism, positron emission tomography kinetics, and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine lesions in primates.
Brain Res. 750(1-2) , 264-76, (1997) The tracer 6-[18F]fluoro-L-m-tyrosine (FMT) was studied with regard to its biochemistry and kinetics, as well as its utility in evaluating brain dopaminergic function in primates before and after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) treatment u... |
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Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination.
Biochemistry 44(10) , 3663-72, (2005) Global replacements of tyrosine by 2- and 3-fluorotyrosine in "enhanced green" and "enhanced yellow" mutants of Aequorea victoria green fluorescent proteins (avGFPs) provided protein variants with novel biophysical properties. While crystallographic and model... |
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Crystallographic evidence for isomeric chromophores in 3-fluorotyrosyl-green fluorescent protein.
ChemBioChem. 5(5) , 720-2, (2004)
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Structural mobility in human manganese superoxide dismutase.
Biochemistry 45(27) , 8209-15, (2006) Human manganese superoxide dismutase (MnSOD) is a homotetramer of 22 kDa subunits, a dimer of dimers containing dimeric and tetrameric interfaces. We have investigated conformational mobility at these interfaces by measuring amide hydrogen/deuterium (H/D) exc... |
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High-efficiency incorporation in vivo of tyrosine analogues with altered hydroxyl acidity in place of the catalytic tyrosine-14 of Delta 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: effects of the modifications on isomerase kinetics.
Biochemistry 37(27) , 9738-42, (1998) Versions of the Y55F/Y88F modified form of Delta 5-3-ketosteroid isomerase in which the active-site tyrosine-14 is replaced by 2-fluorotyrosine, 3-fluorotyrosine, and 2,3-difluorotyrosine, amino acids having progressively greater acidity of their phenolic hyd... |
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Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.
Biochemistry 36 , 10517-10525, (1997) The primary role of Tyr225 in the aspartate aminotransferase mechanism is to provide a hydrogen bond to stabilize the 3'O- functionality of bound pyridoxal phosphate. The strength of this hydrogen bond is perturbed by replacement of Tyr225 with 3-fluoro-L-tyr... |
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Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and [19F]NMR studies.
FEBS Lett. 374(2) , 165-8, (1995) The use of 3-fluoro-tyrosine as an alternative substrate for the enzyme tubulin:tyrosine ligase which catalyzes the incorporation of tyrosine into the alpha-tubulin subunit was investigated. The incorporation of tyrosine into tubulin was inhibited competitive... |