Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13

Alan S. Gelbard; Arthur J.L. Cooper; Yasuhisa Asano; Edward Nieves; Sabina Filc-Dericco; Karen C. Rosenspire

doi:10.1016/0883-2889(90)90114-V

Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13

Alan S. Gelbard, Arthur J.L. Cooper, Yasuhisa Asano, Edward Nieves, Sabina Filc-Dericco, Karen C. Rosenspire

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Abstract

l-[¹³N]Tyrosine and l-[¹³N]phenylalanine were synthesized using immobilized enzymes by two methods. In method 1, [¹³N]ammonia is converted to l-[¹³N]glutamate; transamination with p-hydroxyphenylpyruvate yields l-[¹³N]tyrosine. [¹³N]Tyrosine is separated from other labeled intermediates on a Poropak Q column. In method 2, phenylalanine dehydrogenase catalyzes the reversible reductive [¹³N]amination of either phenylpyruvate or p-hydroxyphenylpyruvate to form l-[¹³N]phenylalanine or l-[¹³N]tyrosine, respectively. The feasibility of labeling DOPA and tryptophan with ¹³N was also demonstrated.

Original language	English (US)
Pages (from-to)	229-233
Number of pages	5
Journal	International Journal of Radiation Applications and Instrumentation. Part
Volume	41
Issue number	2
DOIs	https://doi.org/10.1016/0883-2889(90)90114-V
State	Published - 1990
Externally published	Yes

ASJC Scopus subject areas

Radiation
General Engineering

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@article{5c5273e1aa864ebc837fb34c4aeebe3f,

title = "Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13",

abstract = "l-[13N]Tyrosine and l-[13N]phenylalanine were synthesized using immobilized enzymes by two methods. In method 1, [13N]ammonia is converted to l-[13N]glutamate; transamination with p-hydroxyphenylpyruvate yields l-[13N]tyrosine. [13N]Tyrosine is separated from other labeled intermediates on a Poropak Q column. In method 2, phenylalanine dehydrogenase catalyzes the reversible reductive [13N]amination of either phenylpyruvate or p-hydroxyphenylpyruvate to form l-[13N]phenylalanine or l-[13N]tyrosine, respectively. The feasibility of labeling DOPA and tryptophan with 13N was also demonstrated.",

author = "Gelbard, {Alan S.} and Cooper, {Arthur J.L.} and Yasuhisa Asano and Edward Nieves and Sabina Filc-Dericco and Rosenspire, {Karen C.}",

note = "Funding Information: Acknowledgements-Thiwso rk was supported m part by National Institutes of Health Grants CA-34603 and DK-16739a nd Department of Energy Grant DE-FG-02-86-ER-60407. The authors thank the Memorial Sloan-Kettering Cancer Center Cyclotron Core Facility for the production of nitrogen-13.",

year = "1990",

doi = "10.1016/0883-2889(90)90114-V",

language = "English (US)",

volume = "41",

pages = "229--233",

journal = "International Journal of Radiation Applications and Instrumentation. Part",

issn = "0883-2889",

publisher = "Elsevier Limited",

number = "2",

}

TY - JOUR

T1 - Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13

AU - Gelbard, Alan S.

AU - Cooper, Arthur J.L.

AU - Asano, Yasuhisa

AU - Nieves, Edward

AU - Filc-Dericco, Sabina

AU - Rosenspire, Karen C.

N1 - Funding Information: Acknowledgements-Thiwso rk was supported m part by National Institutes of Health Grants CA-34603 and DK-16739a nd Department of Energy Grant DE-FG-02-86-ER-60407. The authors thank the Memorial Sloan-Kettering Cancer Center Cyclotron Core Facility for the production of nitrogen-13.

PY - 1990

Y1 - 1990

N2 - l-[13N]Tyrosine and l-[13N]phenylalanine were synthesized using immobilized enzymes by two methods. In method 1, [13N]ammonia is converted to l-[13N]glutamate; transamination with p-hydroxyphenylpyruvate yields l-[13N]tyrosine. [13N]Tyrosine is separated from other labeled intermediates on a Poropak Q column. In method 2, phenylalanine dehydrogenase catalyzes the reversible reductive [13N]amination of either phenylpyruvate or p-hydroxyphenylpyruvate to form l-[13N]phenylalanine or l-[13N]tyrosine, respectively. The feasibility of labeling DOPA and tryptophan with 13N was also demonstrated.

AB - l-[13N]Tyrosine and l-[13N]phenylalanine were synthesized using immobilized enzymes by two methods. In method 1, [13N]ammonia is converted to l-[13N]glutamate; transamination with p-hydroxyphenylpyruvate yields l-[13N]tyrosine. [13N]Tyrosine is separated from other labeled intermediates on a Poropak Q column. In method 2, phenylalanine dehydrogenase catalyzes the reversible reductive [13N]amination of either phenylpyruvate or p-hydroxyphenylpyruvate to form l-[13N]phenylalanine or l-[13N]tyrosine, respectively. The feasibility of labeling DOPA and tryptophan with 13N was also demonstrated.

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DO - 10.1016/0883-2889(90)90114-V

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JO - International Journal of Radiation Applications and Instrumentation. Part

JF - International Journal of Radiation Applications and Instrumentation. Part

IS - 2

ER -

Methods for the enzymatic synthesis of tyrosine and phenylalanine labeled with nitrogen-13

Abstract

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