منابع مشابه
Tyrosine Phenol Lyase
Crystalline I,-tyrosine phenol lyase of Escherichia infermedia A-21 is inactive in the absence of added pyridoxal phosphate. Half-maximal enzymatic activity is obtained at a concentration of 1.3 x 10pB M pyridoxal phosphate. Binding of pyridoxal phosphate to the apoenzyme is accompanied by pronounced increase in absorbance at 340 and 430 rng. Holotyrosine phenol lyase requires K+ or NH4+ for it...
متن کاملThree-dimensional structure of tyrosine phenol-lyase.
Tyrosine phenol-lyase (EC 4.1.99.2) from Citrobacter freundii has been cloned and the primary sequence deduced from the DNA sequence. From the BrCN digest of the NaBH4-reduced holoenzyme, five peptides were purified and sequenced. The amino acid sequences of the peptides agreed with the corresponding parts of the tyrosine phenol-lyase sequence obtained from the gene structure. K257 is the pyrid...
متن کاملConversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
Tyrosine phenol-lyase (TPL), which catalyzes the beta-elimination reaction of L-tyrosine, and aspartate aminotransferase (AspAT), which catalyzes the reversible transfer of an amino group from dicarboxylic amino acids to oxo acids, both belong to the alpha-family of vitamin B6-dependent enzymes. To switch the substrate specificity of TPL from L-tyrosine to dicarboxylic amino acids, two amino ac...
متن کاملStudies on tyrosine phenol lyase. Modification of essential histidyl residues by diethylpyrocarbonate.
Tyrosine phenol-lyase of Escherichia intermedia is inactivated by treatment with diethylpyrocarbonate at pH 6.0 AND 4 degrees. Spectrophotometric studies show that the inactivation is stoichiometric, with a modification of 2 histidyl residues per molecule of the enzyme. Finding that this inactivation is largely reversed by treatment with hydroxylamine indicates that the inactivation is mainly d...
متن کاملStereochemistry and mechanism of reactions catalyzed by tyrosine phenol-lyase from Escherichia intermedia.
Stereochemical studies on tyrosine phenol-lyase from Escherichia intermedia have shown that the alpha, beta-elimination reactions of L-serine and D- and L-tyrosine proceed with retention of configuration at C-beta. Stereospecifically beta-tritiated L-serine is slowly racemized at C-beta. Deuterium from the alpha-position of L-tyrosine is partially transferred to C-4 of the phenol formed when th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77159-2