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Tyrosine Decarboxylase, Holoenzyme

Cat no: T9238

Tyrosine Decarboxylase, Holoenzyme

Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary coenzyme. By utilizing the apoenzyme (TYDAPO), prepared from cells grown on a vitamin B6 deficient medium, pyridoxal phosphate may be determined. Decarboxylation of radio-labeled tyrosine has permitted the determination of much smaller amounts of pyridoxal phosphate. \n\nAcetone-dried cells were used as the source in a relatively simple extraction and purification of the apoenzyme. The holoenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically. Tashian (1957) has reported a determination of tyrosine in urine based on this principle. Plasma phenylalanine can also be determined using this enzyme. Poisner (1960) determined serum phenylalanine levels in schizophrenics using Hsia

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SPECIFICATIONS

Catalog Number

T9238

Size

25U

Form

Supplied as lyophilized cells.

Purity

Quality Control: SDS-PAGE

References

1. Bellamy, W. and Gunsalus, I., J. Bact. 50: 95 (1945). 2. Boeker, E. and Snell, E., Amino Acid Decarboxylases, in The Enzymes, VI, 3rd ed., (Boyer, P., ed.), Academic Press, NY, 217 (1972). 3. Chabner, B. and Livingston, D., Anal. Biochem. 34: 413 (1970). 4. Epps, H., Biochem. J. 38: 242 (1944). 5. Gale, E., Meth. Biochem. Anal., IV: 285 (1954). 6. Gale, E., Biochem. J. 41: vii (1957). 7. Gunsalus, I. and Smith, R., Assay and Preparation of Pyridoxal Phosphate, in Methods in Enzymology, III, (Colowick, S., and kaplan, N., eds.), Academic Press, NY, 963 (1957). 8. Hsia, D., Laboratory Methods, in Inborn Errors of Metabolism, Yearbook Publishers, Chicago, 304 (1959). 9. Knox, W. and Messinger, E., Amer. J. Human Genetics 10: 53 (1958). 10. Maruyama, H. and Coursin, D., Anal. Biochem. 26: 420 (1968). 11. Najaar, V., Determination of Amino Acids by Specific Bacterial Decarboxylases in the Warburg Apparatus, in, Methods in Enzymology, III, (Colowick, S., and Kaplan, N., eds.), Academic Press, NY, 462 (1957). 12. Poisner, A., J. Nerv. Ment. Dis. 131: 74 (1960). 13. Snell, E. and Di Mari, S., Schiff Base Intermediates in Enzyme Catalysis, in The Enzymes, II, 3rd ed., (Boyer, P., ed.), Academic Press, NY, 335 (1970). 14. Sundaresan, P. and Coursin, D., Microassay of Pyridoxal Phosphate Using L-Tyrosine-I-14C and Tyrosine Apodecarboxylase, in Methods in Enzymology, XVIIIA, (McCormick, D., and Wright, L., eds.), Academic Press, NY, 509 (1970). 15. Tashian, R., Clin. Chem., 3: 106 (1957). 16. Udenfriend, S. and Cooper, J., J. Biol. Chem. 203: 953 (1953). 17. Umbreit, W., et al., Arch. Biochem., 7: 185 (1945). 18. Vederas, J., et al., J. Biol. Chem. 254: 5053 (1979).

Alternative Names

EC=4.1.1.25; Streptococcus faecalis

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Applications

ELISA

Reactivities

Hum

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Applications

IF

Hosts

Mouse

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Applications

ELISA, WB

Hosts

Mouse

Reactivities

Hum

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Applications

ELISA, FC, WB

Hosts

Mouse

Reactivities

Hum

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Applications

ELISA, FC, IHC, WB

Hosts

Mouse

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Applications

IHC, WB

Hosts

Rabbit

Reactivities

Hum

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Applications

ELISA, WB

Hosts

Rabbit

Reactivities

Hum

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