[87] Fructose diphosphate aldolase

Rutter, William J.; Hunsley, James R.; Groves, William E.; Calder, John H.; Rajkumar, T; Woodfin, Beulah M.

doi:10.1016/0076-6879(66)09099-2

Cited by 80 publications

(52 citation statements)

References 25 publications

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“…Ferritins isolated from normal and Cd2+-or Zn2+-injected animals are abbreviated as ferritin-control, ferritin-Cd, and ferritin-Zn, respectively. Yeast phosphoglucomutase was isolated from Fleischmann's yeast as described (8) and aldolase was isolated as described by Rutter and Hunsley (9). Calf intestinal alkaline phosphatase was purchased from Sigma.…”

Section: Methodsmentioning

confidence: 99%

Ferritin: a zinc detoxicant and a zinc ion donor.

Price¹,

Joshi²

1982

Proc. Natl. Acad. Sci. U.S.A.

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Rats were injected with 1 mg of Zn2' as zinc sulfate or 2 mg of Cd2+ as cadmium sulfate per kg of body weight on a daily basis. After seven injections, ferritin and metallothionein were isolated from the livers of the rats. Significant amounts of zinc were associated with ferritin. Incubation ofsuch ferritin with apoenzymes of calf intestinal alkaline phosphatase, yeast phosphoglucomutase, and yeast aldolase restored their enzymic activity. The amount of zinc injected was insufficient to stimulate significant synthesis ofmetallothionein, but similar experiments with injection of cadmium did stimulate the synthesis of metallothionein. The amount of Zn2`in ferritin of Cd-injected rats was greater than that in ferritin in Zn-injected rats, which was greater than that in ferritin of normal rats. Thus at comparable protein concentration ferritin from Cd-injected rats was a better. Zn2+ donor than was ferritin from Zn-injected or normal animals. Ferritin is a normal constituent of several tissues, whereas metallothionein is synthesized under metabolic stress. Thus ferritin may function as a "metal storage and transferring agent" for iron and for zinc. It is su gested that ferritin probably serves as the initial chelator for Zn + and perhaps other metal ions as well and that under very high toxic levels of metal ions the synthesis of metallothionein is initiated as the second line of defense.

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Section: Methodsmentioning

confidence: 99%

Ferritin: a zinc detoxicant and a zinc ion donor.

Price¹,

Joshi²

1982

Proc. Natl. Acad. Sci. U.S.A.

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“…Enzyme activities were determined with coupled optical tests. As substrates were used fructose 1,6-bisphosphate in the assay for muscle aldolase [19] and yeast aldolase [20]; fructose 6-phosphate plus erythrose 4-phosphate for transaldolase [21], and xylulose 5-phosphate plus ribose 5-phosphate for transketolase [22]. All activity assays were performed at 25 "C. Muscle aldolase concentration was determined from the absorbance at 280 nm, A : = 0.91 [23].…”

Section: Methodsmentioning

confidence: 99%

Specific Irreversible Inhibition of Enzymes Concomitant to the Oxidation of Carbanionic Enzyme · Substrate Intermediates by Hexacyanoferrate(III)

Christen

Cogoli-Greuter

Healy

et al. 1976

European Journal of Biochemistry

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Four different enzymes, class I fructose-l,6-bisphosphate aldolase from rabbit muscle, class I1 fructose-l,6-bisphosphate aldolase from yeast, transaldolase, and transketolase, are inactivated progressively in the presence of their specific substrates and hexacyanoferrate(II1). The inactivation is strictly linked to the oxidation of the carbanionic enzyme . substrate intermediates of these enzymes reported previously [Healy, M. J. and Christen, P. (1973) Biochemistry, 12, 351. However, the loss of activity is not due to the products of this oxidation, i.e. to hexacyanoferrate(II), or to the oxidation product of the substrate such as hydroxypyruvaldehyde phosphate in the case of aldolase The rate of inactivation is independent of the concentration of the enzyme, suggesting that the inactivation results from an intramolecular reaction, i.e. the inactivating agent produced by oxidation of the enzyme . substrate intermediate is not released from the active site but rather reacts in situ with the enzyme protein. Accordingly, addition of fructose 1,6-bisphosphate to a mixture of aldolase and transaldolase (or transketolase) with hexacyanoferrate(II1) initiates the exclusive inactivation of aldolase while the addition of fructose 6-phosphate induces the exclusive inactivation of transaldolase (or transketolase respectively).The combination of natural substrate with hexacyanoferrate(II1) thus constitutes a binary system for the chemical modification of enzymes that form oxidizable carbanionic intermediates. The modification by oxidative activation of enzyme . substrate intermediates is (a) highly specific for a given enzyme (the degree of specificity is determined by the binding and kinetic specificity of the enzyme for its natural substrate) and (b) results in a modification of groups at or near the enzyme's active site (reaction of the oxidatively activated substrate in situ).

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“…6) form a group, with corresponding Z values of about seven, followed by the liver aldolases (type B, Fig. 6 20 min observed under conditions of antibody saturation. These maximum levels of antibody binding were obtained from doublereciprocal plots of ELISA data (see Fig.…”

Section: Structural Similarities Between the Cytosolic And Chloroplasmentioning

confidence: 99%

“…The class II (metallo) aldolase derived from yeast was purified about 10-fold by ammonium sulfate fractionation using a procedure similar to that originally described by Rutter and co-workers (20). Yeast cakes were suspended in 50 mM 2-mercaptoethanol, 0.1 mm ZnSO4, 0.2 mM PMSF, and the cells were harvested by centrifugation at 10,000g for 10 min.…”

Section: Purification Of Fructose Bisphosphate Aldolasesmentioning

confidence: 99%

Structural Similarities between Spinach Chloroplast and Cytosolic Class I Fructose 1,6-Bisphosphate Aldolases

Marsh

Wilson²,

Lebherz³

1989

Plant Physiol.

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Immunochemical studies using polyclonal antisera prepared individually against highly purified cytosolic and chloroplast spinach leaf (Spinacia oleracea) fructose bisphosphate aldolases showed significant cross reaction between both forms of spinach aldolase and their heterologous antisera. The individual cross reactions were estimated to be approximately 50% in both cases under conditions of antibody saturation using a highly sensitive enzyme-linked immunosorbent assay. In contrast, the class I procaryotic aldolase from Mycobacterium smegmatis and the class 11 aldolase from yeast (Saccharomyces cerevisiae) did not cross-react with either type of antiserum. The 29 residue long amino-terminal amino acid sequences of the procaryotic M. smegmatis and the spinach chloroplast aldolases were determined. Comparisons of these sequences with those of other aldolases showed that the amino-terminal primary structure of the chloroplast aldolase is much more similar to the amino-terminal structures of class I cytosolic eucaryotic aldolases than it is to the corresponding region of the M. smegmatis enzyme, especially in that region which forms the first "beta sheet" in the secondary structure of the eucaryotic aldolases. Moreover, results of a systematic comparison of the amino acid compositions of a number of diverse eucaryotic and procaryotic fructose bisphosphate aldolases further suggest that the chloroplast aldolase belongs to the eucaryotic rather than the procaryotic "family" of class I aldolases.One of the most striking distinctions between eucaryotic and procaryotic life forms is the complexity of their intracellular architectures. In contrast to procaryotes, most eucaryotic cells contain specialized membrane-limited intracellular organelles in which specific biochemical pathways are compartmentalized. For example, reactions of the Krebs cycle and those of the oxidative phosphorylation pathway occur in mitochondria while the "light" and "dark" reactions of photosynthesis take place within chloroplast organelles of photosynthetic eucaryotes. Many glycolytic enzymes in the leaves of higher plants exist as enzyme "pairs," one member of the pair residing in the cytosol and the other member sequestered within the chloroplast organelle (8,26 (14) showed that the cytosolic and chloroplast forms of spinach leaf aldolase exhibit similar specific catalytic activities and appear to possess functional carboxy-terminal structures. However, they are distinctive on the basis of charge, subunit molecular weight, thermal stability, amino acid composition, tryptic peptide patterns and immunological properties. Hence, the two spinach leaf enzymes are presumably the products of different structural genes.All aldolases are further categorized as being either class I or class II enzymes depending on the mechanism they utilize for the cleavage of fructose bisphosphate to triose phosphates (19)

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[87] Fructose diphosphate aldolase

Cited by 80 publications

References 25 publications

Ferritin: a zinc detoxicant and a zinc ion donor.

Ferritin: a zinc detoxicant and a zinc ion donor.

Specific Irreversible Inhibition of Enzymes Concomitant to the Oxidation of Carbanionic Enzyme · Substrate Intermediates by Hexacyanoferrate(III)

Structural Similarities between Spinach Chloroplast and Cytosolic Class I Fructose 1,6-Bisphosphate Aldolases

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