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N ‐Acetylation of L‐Aspartate in the Nervous System: Differential Distribution of a Specific Enzyme
Author(s) -
Truckenmiller M. E.,
Namboodiri M. A. A.,
Brownstein M. J.,
Neale J. H.
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb07240.x
Subject(s) - enzyme , enzyme assay , biochemistry , nervous system , acetylation , central nervous system , kidney , spinal cord , aspartic acid , glutamate receptor , chemistry , acetyltransferase , biology , endocrinology , amino acid , neuroscience , receptor , gene
L‐Aspartate N ‐acetyltransferase, a nervous system enzyme that mediates the synthesis of N ‐acetyl‐L‐aspartic acid, has been characterized. In the presence of acetyl‐CoA, L‐aspartate was acetylated 10‐fold more efficiently than L‐glutamate, and the acetylation of aspartylglutamate was not detectable. Within the nervous system, a 10‐fold variation in the enzyme activity was observed, with the brainstem and spinal cord exhibiting the highest activity (10–15 pmol/min/mg tissue) and retina the lowest detectable activity (1–1.5 pmol/min/mg). No enzyme activity was detected in pituitary, heart, liver, or kidney. The enzyme activity was found to be membrane‐associated and was solubilized by treatment with Triton X‐100.