In:
Journal of Neurochemistry, Wiley, Vol. 30, No. 6 ( 1978-06), p. 1261-1267
Abstract:
Abstract— The catalytic activity of γ‐glutamyl transpeptidase (γ‐GTP) from bovine choroid plexus has been shown to be subject to modulation by a variety of effectors. L‐Alanine and L‐serine not only functioned as acceptor substrates to which γ‐glutamyl moieties could be transferred, but also as noncom‐petitive inhibitors of the reaction in the presence of the dipeptide acceptor substrate glycylglycine. In contrast, D‐alanine does not function as an acceptor substrate, but does noncompetitively inhibit the transfer of γ‐glutamyl groups to glycylglycine. Similarly, borate ions inhibited y‐GTP noncompetitively, while a mixture of L‐serine and borate were potent uncompetitive inhibitors of the reaction with a K i of 0.6 mM. Several dicarboxylic acids, including maleate, maleylglycine, and malonate, inhibited γ‐GTP; this inhibition was acceptor substrate‐dependent. The inhibition of γ‐GTP by maleate was competitive with respect to the acceptor substrate glycylglycine.
Type of Medium:
Online Resource
ISSN:
0022-3042
,
1471-4159
DOI:
10.1111/jnc.1978.30.issue-6
DOI:
10.1111/j.1471-4159.1978.tb10454.x
Language:
English
Publisher:
Wiley
Publication Date:
1978
detail.hit.zdb_id:
2020528-4
SSG:
12
