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- W2019643708 abstract "Mouse α- and γ-nerve growth factor (NGF) are glandular kallikreins that form a non-covalent complex (7S NGF) with β-NGF. γ-NGF is an active arginine-specific esteropeptidase; the α-subunit is catalytically inactive and has a zymogen-like conformation. Site-directed mutagenesis of α-NGF to alter the N-terminus and three residues in loop 7, a region that contributes to the catalytic center, restored substantial catalytic activity against N-benzoyl arginine-p-nitroanilide as substrate in two derivatives although they were not as active as recombinant γ-NGF. Seven of the 15 derivatives that remained more α-like were able to substitute for native α-NGF in reforming 7S complexes; the other eight derivatives that were more γ-like showed greatly reduced ability to do so. However, the most γ-like α-NGF derivative could not substitute for native γ-NGF in 7S complex formation. These findings suggest that the α-NGF backbone can be corrected to a functional enzyme by the addition of a normal N-terminal structure and two catalytic site substitutions and that the 7S complex requires one kallikrein subunit in the zymogen form and one in an active conformation." @default.
- W2019643708 created "2016-06-24" @default.
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- W2019643708 date "2000-03-01" @default.
- W2019643708 modified "2023-10-14" @default.
- W2019643708 title "Nerve growth factor α subunit: effect of site-directed mutations on catalytic activity and 7S NGF complex formation" @default.
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- W2019643708 doi "https://doi.org/10.1016/s0167-4838(99)00277-0" @default.
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