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The occurrence of N ‐acetylaspartate amidohydrolase (Aminoacylase II) in the developing rat 1
Author(s) -
D'Adamo A. F.,
Smith J. Crispin,
Woiler C.
Publication year - 1973
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.1471-4159.1973.tb00097.x
Subject(s) - amidohydrolase , enzyme , biochemistry , biology , amino acid , medicine , aspartic acid , kidney , endocrinology , stereochemistry , chemistry
O f T he amino acids and derivatives, N ‐acetyl‐L‐aspartic acid is present in a uniquely high level (5–6 μmol/g) in the brain of mammals after myelination has occurred. Much lower levels (0·06–0·17 μmol/g) are found prior to this stage of brain development (T allan , 1957). In non‐nervous tissues, on the other hand, only trace amounts of this acetyl amino acid are present (T allan , M oore and S tein , 1956). N ‐acetyl aspartic acid serves as an excellent source of acetyl groups for lipogenesis in the developing rat brain (D'A damo and Y atsu , 1966; D adamo , G idez and Y atsu , 1968). Non‐nervous tissues such as kidney and mammary gland also rapidly metabolize the acetyl amino acid, the former tissue converting the acetyl group primarily to CO 2 and the latter to fatty acids (B enuck and D'A damo , 1968). An enzyme with a high specificity for N‐acetyl‐L‐aspartic acid initially termed aminoacylase II, was originally isolated from hog kidney by B irnbaum et al. (1952). Since the physiological role of the substrate is not known, it was of interest to study the occurrence of this enzyme, N ‐acetyl‐L‐aspartate amidohydrolase (EC 3.5.1.15), in developing tissues of the rat.