Enzymic formation of di-D-fructose anhydrides from fructan.
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چکیده
منابع مشابه
Enzymic formation of D-malate.
Tubbs & Greville (1961) showed that D-2hydroxy acid dehydrogenase (EC 1.1.2.4), present in liver and kidney in several animal species, catalyses the oxidation of D-lactate, D-malate and various straight-chain homologues. Similar NADindependent D-lactate dehydrogenases have been isolated from micro-organisms (Haugaard, 1959; de Ley & Schel, 1959; Snoswell, 1959; Nygaard, 1960). However, the meta...
متن کاملThe enzymic hydrolysis of acid anhydrides.
Aebi, H. (1953). Helv. physiol. acta, 11, 96. Boyd, G. E., Schubert, J. & Adamson, A. W. (1947). J. Amer. chem. Soc. 69, 2818. Conway, E. J. & Hingerty, D. (1946). Biochem. J. 40, 561. Conway, E. J. & McCormack, J. I. (1953). J. Physiol. 120, 1. Davies, F., Davies, R. E., Francis, E. T. B. & Whittam, R. (1952). J. Physiol. 118, 276. Deutsch, W. (1936). J. Physiol. 87, 56P. Domingo, W. R. & Klyn...
متن کاملFormation of stable anhydrides from CoA transferase and hydroxamic acids.
Acetohydroxamic acid reacts with the enzyme-CoA form of succinyl-CoA:3-ketoacid coenzyme A transferase to give an inactive product with a rate constant of 860 M-1 min-1 at pH 8.1, 25 degrees C. The reaction is reversible in the presence of coenzyme A and has an equilibrium constant of 0.040. The product is an anhydride that is an analog of the intermediate that has been postulated in the normal...
متن کاملEnzymic formation of p-hydroxybenzoate from p-hydroxycinnamate.
An enzyme that converts p-hydroxycinnamate into p-hydroxybenzoate was found in rat liver. It is localized in the mitochondria and requires ATP. The activity is lost when the mitochondria are stored frozen overnight. Addition of magnesium chloride, cytochrome c, GSH, coenzyme A or potassium cyanide did not have any effect on the activity. When the rats were fed with alpha-p-chlorophenoxyisobutyr...
متن کاملPARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA
The first enzyme of the pathway for uridine diphosphate N-acetyl-D-glucosamine (UDPAG) biosynthesis i.e. L-glutamine: D-fructose 6-P amidotransferase (E.C. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on DEAE-Sephadex A-50. The enzyme showed optimal activity in a broad range of pH from 5.8 to 7.8 in both phosphate and cacodylate ...
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ژورنال
عنوان ژورنال: Journal of the Japanese Society of Starch Science
سال: 1988
ISSN: 1884-488X,0021-5406
DOI: 10.5458/jag1972.35.113