An allosteric α-glucan phosphorylase from banana fruits

Singh, Surjeet; Sanwal, G.G.

doi:10.1016/0005-2744(73)90026-0

Cited by 16 publications

(6 citation statements)

References 17 publications

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“…Ammonium sulfate fractionation of the initial extract followed by chromatography on DEAE-cellulose and gel filtration through Sephadex G-100 and Sephadex G-200 resulted in 110-fold purification of starch phosphorylase with 28% recovery from the initial extract. The specific activity of the enzyme (27.8) was about */u that of the potato enzyme (Kamogawa et al, 1968), about '/u of banana fruit (Singh & Sanwal, 1973), about '/io of the cytoplasmic spinach leaf enzyme (Steup et al, 1980a), about '/4 of the chloroplastic spinach leaf enzyme (Steup, 1981), and about */7 of pea seed (Matheson & Richardson, 1978) phosphorylase. The further purification of the enzyme by affinity chromatography using starch-bound Sepharose-4B did not increase the specific activity of starch phosphorylase.…”

Section: Resultsmentioning

confidence: 95%

“…The Km values of starch phosphorylases from various sources for glucose 1-phosphate have been reported in the range 0.6-5 mM and those for inorganic phosphate 1-10 mM (Tsai & Nelson, 1968;Gold et al, 1971;Lee & Braun, 1973;Singh & Sanwal, 1973Ariki & Fukui, 1975b; Burr & Nelson, 1975;Preiss et al, 1980). A large difference in the Km values of starch phosphorylases for the primer has been reported.…”

Section: Discussionmentioning

confidence: 99%

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Purification and physicochemical properties of starch phosphorylase from young banana leaves

Kumar¹,

Sanwal²

1982

Biochemistry

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Starch phosphorylase from young banana leaves has been purified to homogeneity, as tested by disc polyacrylamide gel electrophoresis at various pHs and gel concentrations, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunodiffusion, and immunoelectrophoresis, using the techniques of ammonium sulfate fractionation, DEAE-cellulose chromatography, and filtration through Sephadex G-100 and Sephadex G-200. The molecular weight of the enzyme is found to be 45000 as determined by gel filtration chromatography over Sephadex G-200. The enzyme showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis having the molecular weight 55000. The enzyme contains eight SH groups per mol of the enzyme. Unlike other 1,4-alpha-glucan phosphorylases, no evidence is found for the presence of pyridoxal 5'-phosphate as a prosthetic group of the enzyme. Of the various amino acids tested, only aromatic amino acids inhibited the enzyme activity. ADP, AMP, and 3',5'-AMP did not produce any effect on the enzyme activity whereas ATP and UDP-glucose proved to be inhibitors. The enzyme utilized starch, amylose, and glycogen as primers with equal efficiency whereas dextrin, amylopectin, maltotriose, and maltose were less effective as primers. Schardinger dextrin, cellulose, or sucrose could not be utilized as a primer. The enzyme showed absolute specificity for glucose 1-phosphate as a substrate, and this could not be replaced by glucose-6-phosphate, fructose-6-phosphate, fructose 1,6-bisphosphate, or ribose 5-phosphate.

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Section: Resultsmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Purification and physicochemical properties of starch phosphorylase from young banana leaves

Kumar¹,

Sanwal²

1982

Biochemistry

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“…Since aromatic amino acids, in principle, are originally derived from starch, we believe that by inhibition, they may exert a control via negative feedback mechanisms (Kumar and Sanwal, 1988). The allosteric mechanism of SP by l-tyrosine and ATP has also been demonstrated (Singh and Sanwal, 1973;Kumar andSanwal, 1983b, 1988).…”

Section: Regulation Of Starch Phosphorylase Activitiesmentioning

confidence: 90%

Starch phosphorylase: Role in starch metabolism and biotechnological applications

Rathore¹,

Garg²,

Garg³

et al. 2009

Critical Reviews in Biotechnology

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The alpha-glucan phosphorylases of the glycosyltransferase family are important enzymes of carbohydrate metabolism in prokaryotes and eukaryotes. The plant alpha-glucan phosphorylase, commonly called starch phosphorylase (EC 2.4.1.1), is largely known for the phosphorolytic degradation of starch. Starch phosphorylase catalyzes the reversible transfer of glucosyl units from glucose-1-phosphate to the nonreducing end of alpha-1,4-D-glucan chains with the release of phosphate. Two distinct forms of starch phosphorylase, plastidic phosphorylase and cytosolic phosphorylase, have been consistently observed in higher plants. Starch phosphorylase is industrially useful and a preferred enzyme among all glucan phosphorylases for phosphorolytic reactions for the production of glucose-1-phosphate and for the development of engineered varieties of glucans and starch. Despite several investigations, the precise functional mechanisms of its characteristic multiple forms and the structural details are still eluding us. Recent discoveries have shed some light on their physiological substrates, precise biological functions, and regulatory aspects. In this review, we have highlighted important developments in understanding the role of starch phosphorylases and their emerging applications in industry.

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“…A similar observation was made by Surendranatham and Nair (18) but for earlier stages of ripening. Singh and Sanwall (15,16,17) partially purified three phosphorylase forms from ripe bananas and observed different biochemical characteristics but did not investigate the behavior of these enzymes during ripening.…”

Section: They Also Detected the Presence Of P-amylase And Phosphorylasementioning

confidence: 99%

“…When the genetic base of a breeding program is very narrow, however, inbreeding may be difficult to avoid. A limited number of parents have been extensively used, for example, in the breeding of raspberries (15), peaches (11), cherries (9), and, to a lesser extent, apples (8 ).…”

Section: Response Of Pear To Inbreeding1mentioning

confidence: 99%

Phosphorylase, Phosphatase, α-Amylase Activity and Starch Breakdown during Ripening of ‘Marmelo’ Banana [(Musa acuminata Colla) × (Musa balbisiana Colla) ABB Group] Whole Fruit and Thin Slices1

Chitarra

Lajolo²

1981

J. Amer. Soc. Hort. Sci.

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Starch hydrolysis, phosphorylase, phosphatase and α-amylase activity of ‘Marinelo’ banana (Musa acuminata Colla × Musa balbisiana Colla, ABB group) during ripening of whole fruit and thin slices infiltrated with water (controls), cycloheximide and actinomycin D were investigated. Phosphatase and α-amylase activity of whole fruit increased during the climacteric while phosphorylase decreased as starch degradation proceded. Starch degradation had a different temperature coefficient than that of α-amylase activity when the storage temperature was raised from 20 to 25°C and stopped when 25% of the starch was still present. Activity of α-amylase in slices infiltrated with water, increased before the onset of the climacteric as a result of injury and at the same time starch was being hydrolyzed. Cycloheximide inhibited this induced activity increase but not starch breakdown or the increase of activity which occurs during the climacteric. Actinomycin D did not inhibit the α-amylase increase and its effect was a general retardation of ripening.

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An allosteric α-glucan phosphorylase from banana fruits

Cited by 16 publications

References 17 publications

Purification and physicochemical properties of starch phosphorylase from young banana leaves

Purification and physicochemical properties of starch phosphorylase from young banana leaves

Starch phosphorylase: Role in starch metabolism and biotechnological applications

Phosphorylase, Phosphatase, α-Amylase Activity and Starch Breakdown during Ripening of ‘Marmelo’ Banana [(Musa acuminata Colla) × (Musa balbisiana Colla) ABB Group] Whole Fruit and Thin Slices1

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