The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming).
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منابع مشابه
The reaction of pyridoxal 5'-phosphate with an essential lysine residue of saccharopine dehydrogenase (L-lysine-forming).
Saccharopine dehydrogenase (EC 1.5.1.7) from bakers’ yeast was reversibly inactivated by pyridoxal and pyridoxal 5’-phosphate. The inactivation by pyridoxal 5’-phosphate was accompanied by the appearance of a peak at 428 nm, which was shifted to 325 nm upon reduction with NaBH4. Paper chromatography of an acid hydrolysate of the pyridoxal 5’-phosphate-treated, NaBH4-reduced enzyme showed the pr...
متن کاملChemical modification of the active site sulfhydryl group of saccharopine dehydrogenase (L-lysine-forming).
Saccharopine dehydrogenase (e-N-(L-glutaryl-2)-L1ysine:NAD oxidoreductase (L-lysine-forming) EC 1.5.1.7) is inhibited by a variety of sulfhydryl reagents. Althoughp-chloromercuribenzoate and 5,5’-dithiobis(2nitrobenzoate) react with three sulfhydryl groups present in the enzyme, reaction with one reactive sulfhydryl group leads to complete loss of catalytic activity. Amino acid analysis of the ...
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Two pathways of lysine biosynthesis are known to exist in nature. The diaminopimelic acid pathway, studied in detail in Escherichia coli (l), is the route of lysine biosynthesis in bacteria, certain lower fungi, algae, and higher plants (2). In other classes of lower fungi, in higher fungi, and in Euglena, lysine is synthesized in a different manner, involving the intermediate cu-aminoadipic ac...
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In plant and mammalian cells, excess lysine is catabolized by a pathway that is initiated by two enzymes, namely, lysine-ketoglutarate reductase and saccharopine dehydrogenase. In this study, we report the cloning of an Arabidopsis cDNA encoding a bifunctional polypeptide that contains both of these enzyme activities linked to each other. RNA gel blot analysis identified two mRNA bands-a large ...
متن کاملLysine Decarboxylase with an Enhanced Affinity for Pyridoxal 5-Phosphate by Disulfide Bond-Mediated Spatial Reconstitution
Lysine decarboxylase (LDC) catalyzes the decarboxylation of l-lysine to produce cadaverine, an important industrial platform chemical for bio-based polyamides. However, due to high flexibility at the pyridoxal 5-phosphate (PLP) binding site, use of the enzyme for cadaverine production requires continuous supplement of large amounts of PLP. In order to develop an LDC enzyme from Selenomonas rumi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)79719-x