Characterization of Chloroplastic Fructose 1,6-Bisphosphate Aldolases as Lysine-methylated Proteins in Plants
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چکیده
منابع مشابه
The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.
Two forms of the enzyme fructoseI ,6-bisphosphate aldolase (EC 4. I .2.13) are known, designated class I and class 11. The enzymes o f class I function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion (for review, see [ I , 21). The enzymes of class I1 utilize a divalent metal ion to act ...
متن کاملA conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.
The aldolase catalytic cycle consists of a number of proton transfers that interconvert covalent enzyme intermediates. Glu-187 is a conserved amino acid that is located in the mammalian fructose-1,6-bisphosphate aldolase active site. Its central location, within hydrogen bonding distance of three other conserved active site residues: Lys-146, Glu-189, and Schiff base-forming Lys-229, makes it a...
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Introduction This report considers the contribution of recent studies on transgenic plants to our current understanding of the role of fructose-2,6-bisphosphate (Fru-2,6-P,) in the regulation of carbon metabolism. From data obtained using such plants we argue that this metabolite is quantitatively important in the control of carbohydrate metabolism in both photosynthetic and non-photosynthetic ...
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The phosphatases that hydrolyze fructose 2,6-bisphosphate in a crude spinach (Spinacia oleracea L.) leaf extract were separated by chromatography on blue Sepharose, into three fractions, referred to as phosphatases I, II, and III, which were further purified by various means. Phosphatase I hydrolyzed fructose 2,6-bisphosphate, with a K(m) value of 30 micromolar, to a mixture of fructose 2-phosp...
متن کاملEffects of fructose 2,6-bisphosphate on phosphoglucomutase from plants.
Fructose 2,6-bisphosphate affects phosphoglucomutase from plant and animal sources in a similar way. As previously found with rabbit muscle phosphoglucomutase, fructose 2,6-bisphosphate cannot substitute for glucose 1,6-bisphosphate as a cofactor in the reaction catalyzed by phosphoglucomutase from potato tubers, pea seeds, and string-beans. In the presence of glucose 1,6-bisphosphate, fructose...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2012
ISSN: 0021-9258
DOI: 10.1074/jbc.m112.359976