Carbohydrate metabolism in citric acid fermentation. 4. Purification and properties of aldolase from <i>Aspergillus niger</i>

Jagannathan, V.; Singh, Kartar; Damodaran, M.

doi:10.1042/bj0630094

Cited by 183 publications

(43 citation statements)

References 9 publications

(5 reference statements)

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“…One unit reduces 1 mol of NADP per min at 25°C. The D-fructose 1,6-bisphosphate aldolase (ALD) activity was determined by a modification of the method of Jagannathan et al (11) in which 3-phosphoglyceraldehyde reacts with hydrazine to form a hydrazone which absorbs at 240 nm. One unit is described as a change in absorbance of 1.00 per min at 25°C and pH 7.5.…”

Section: Methodsmentioning

confidence: 99%

Induction of a Futile Embden-Meyerhof-Parnas Pathway in Deinococcus radiodurans by Mn: Possible Role of the Pentose Phosphate Pathway in Cell Survival

Zhang

Wong

Chen³

et al. 2000

Appl Environ Microbiol

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Statistical models were used to predict the effects of tryptone, glucose, yeast extract (TGY) and Mn on biomass formation of the highly radioresistant bacterium Deinococcus radiodurans. Results suggested that glucose had marginal effect on biomass buildup, but Mn was a significant factor for biomass formation. Mn also facilitated glucose interactions with other nutrient components. These predictions were verified by in vivo and in vitro experiments. TGY-grown cells metabolized glucose solely by the pentose phosphate pathway (PPP). Although only a fraction of glucose from the medium was transported into the cells, glucose was incorporated into the DNA efficiently after cells were exposed to UV light. The presence of glucose also enhanced the radioresistance of the culture. Mn could induce an Embden-Meyerhof-Parnas (EMP) pathway in D. radiodurans. The EMP pathway and the PPP of the Mn-treated cells oxidized glucose simultaneously at a 6:1 ratio. Although glucose was hydrolyzed rapidly by the Mn-treated cells, most glucose was released as CO 2 . Mntreated cultures retained less glucose per cell than cells grown without Mn, and still less glucose was incorporated into the DNA after cells were exposed to UV light. Mn-treated cells were also more sensitive to UV light. Results suggested that metabolites of glucose generated from the PPP enhanced the survival of D. radiodurans. Induction of the EMP pathway by Mn may deplete metabolites for DNA repair and may induce oxidative stress for the cell, leading to reduction of radioresistance.The genus Deinococcus is composed of a group of bacteria characterized by their extreme resistance to ionizing radiation (1,7,9,(17)(18)(19). Most experts agree that Deinococcus radiodurans has a very effective system to repair its DNA, but the molecular basis of this effective system is not clear (14,17,18). It appears that D. radiodurans achieves its resistance to radiation by changing the operating conditions of many "ordinary" enzymes (3). Most researchers use the tryptone-glucose-yeast extract (TGY) medium to grow Deinococcus (American Type Culture Collection catalogue. 1996. American Type Culture Collection, Manassas, Va.) (19), even though these organisms are generally considered inactive to sugars (21). Chou and Tan (5) showed that the addition of Mn to a stationary-phase culture of D. radiodurans could induce new rounds of cell division. They termed this mode of growth Mn-induced cell division (MnCD) and suggested that MnCD is a form of starvation growth (23). The authors also showed that the addition of Mn to the culture also induced higher superoxide dismutase (SOD) and catalase activity in the culture. Interestingly, D. radiodurans also became more sensitive to radiation when Mn was included in the culture. Mn is required in many metabolic enzymes. In D. radiodurans, this element serves as a cofactor of SOD (12). The binding of Mn to the chromosomes of the intact cells may contribute to its resistance to radiation (14). Evans and Moseley (9) suggested that Mn served as a cofac...

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Section: Methodsmentioning

confidence: 99%

Induction of a Futile Embden-Meyerhof-Parnas Pathway in Deinococcus radiodurans by Mn: Possible Role of the Pentose Phosphate Pathway in Cell Survival

Zhang

Wong

Chen³

et al. 2000

Appl Environ Microbiol

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“…3-phosphate Aldolase activity was assayed by the method of Jagannathan et al [9] in the presence of 3 mM fructose 1,6-bisphosphate and 10 mM hydrazine sulphate.…”

Section: Kinetic Mctr Jitrementsmentioning

confidence: 99%

Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase

Kvassman¹,

Pettersson²,

Ryde‐Pettersson³

1988

European Journal of Biochemistry

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The catalytic interaction of glyceraldehyde-3-phosphate dehydrogenase with glyceraldehyde 3-phosphate has been examined by transient-state kinetic methods. The results confirm previous reports that the apparent K , for oxidative phosphorylation of glyceraldehyde 3-phosphate decreases at least 50-fold when the substrate is generated in a coupled reaction system through the action of aldolase on fructose 1,6-bisphosphate, but lend no support to the proposal that glyceraldehyde 3-phosphate is directly transferred between the two enzymes without prior release to the reaction medium. A theoretical analysis is presented which shows that the kinetic behaviour of the coupled two-enzme system is compatible in all respects tested with a free-diffusion mechanism for the transfer of glyceraldehyde 3-phosphate from the producing enzyme to the consuming one.Ovadi and Keleti in 1978 reported that the apparent K , for the catalytic interaction of glyceraldehyde-3-phosphate dehydrogenase with glyceraldehyde 3-phosphate decreases about 50-fold when the substrate is generated in a coupled reaction system through the action of aldolase on fructose 1,6-bisphosphate 111. This effect was attributed to reversible complex formation between the two enzymes, permitting the substrate to be directly transferred from aldolase to glyceraldehyde-3-phosphate dehydrogenase without prior release to the reaction medium. Kinetic evidence claimed to be indicative of a direct transfer of metabolites has later been presented also for coupled two-enzyme reactions involving aldolase and glycerol-3-phosphate dehydrogenase [2], as well as glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase [3], alcohol dehydrogenase [4], or various other dehydrogenases [5].The above reports are of outstanding enzymological interest because they suggest that enzymes in the glycolytic and ancillary pathways might be structurally designed to interact with a protein-substrate complex rather than with a free substrate. They also bring into question inferences provided by the application of modern control theory [6, 71 for analysis of the dynamic behaviour and regulation of the glycolytic sequence of reactions ; such analyses invariably have been based on the tacit assumption that metabolite transfer between consecutive enzymes in the glycolytic pathway occurs via the reaction medium through free diffusion. It seems most important, therefore, to ascertain that unambiguous kinetic evidence has been presented to support the proposed existence of mechanisms for direct metabolite transfer in reaction systems involving glycolytic enzymes.

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“…Inhibition was corroborated by monitoring hydrazone formation at 240 nm in a chemical assay based on reaction of hydrazine with the nascent aldehyde (32).…”

mentioning

confidence: 99%

Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli

Santangelo

Gest

Guerin

et al. 2011

Journal of Biological Chemistry

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Background: New drugs active against persistent Mycobacterium tuberculosis are needed. Results: The fructose-1,6-bisphosphate aldolase (FBA-tb) is essential for growth of M. tuberculosis, is expressed by replicating and non-replicating bacilli, and displays plasminogen binding activity. Conclusion: FBA-tb is an essential TB enzyme that might also play a role in host/pathogen interactions. Significance: FBA-tb shows potential as a novel anti-TB therapeutic target.

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Carbohydrate metabolism in citric acid fermentation. 4. Purification and properties of aldolase from Aspergillus niger

Cited by 183 publications

References 9 publications

Induction of a Futile Embden-Meyerhof-Parnas Pathway in Deinococcus radiodurans by Mn: Possible Role of the Pentose Phosphate Pathway in Cell Survival

Induction of a Futile Embden-Meyerhof-Parnas Pathway in Deinococcus radiodurans by Mn: Possible Role of the Pentose Phosphate Pathway in Cell Survival

Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase

Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli

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