The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues
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چکیده
منابع مشابه
The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues.
Full-length rat HDC (L-histidine decarboxylase) translated in reticulocyte cell lysate reactions is inactive, whereas C-terminally truncated isoforms are capable of histamine biosynthesis. C-terminal processing of the approximately 74 kDa full-length protein occurs naturally in vivo, with the production of multiple truncated isoforms. The minimal C-terminal truncation required for the acquisiti...
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Molecular modeling analysis of charge density and heat of fornation by PM3 method as well as C, H NMR and 2D-NMR measurements of histidine (substrate) and some of its derivatives as histidine decarboxylase inhibitors were performed. It was established that the atom, usually nitrogen, which forms internal aldimine with pyridoxal5 -phosphate (PLP), (coenzyme), has negative and almost equal ...
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molecular modeling analysis of charge density and heat of fornation by pm3 method as well as c, h nmr and 2d-nmr measurements of histidine (substrate) and some of its derivatives as histidine decarboxylase inhibitors were performed. it was established that the atom, usually nitrogen, which forms internal aldimine with pyridoxal5 -phosphate (plp), (coenzyme), has negative and almost equal charge...
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A pyridoxal 5'-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15 was purified to homogeneity. The enzyme is a tetramer (Mr 170,000) of identical subunits and binds 4 pyridoxal-P/tetramer; it is resolved by dialysis against cysteine at pH 6.8. Between pH 6.2 and 8.8, the holoenzyme shows pH-independent absorbance maxima at 333 and 416 nm. Vmax/Km is highest at pH 6.5; th...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2004
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20031553