Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles

Wooster, M S; Wrigglesworth, John M.

doi:10.1042/bj1590627

Cited by 24 publications

(3 citation statements)

References 18 publications

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“…There is evidence in the literature that enzymes generally accepted as being soluble might function in their native physiological state associated with some intracellular membrane or to the plasma membrane, and, furthermore, that the microenvironment provided by the membranes might affect their activity (Wilson, 1968;McLaren and Packer, 1970;Katchalski et al, 1971;Solomon and Miller, 1976;Wooster and Wrigglesworth, 1976). Although subcellular fractionation studies of GAD indicate that this enzyme is mainly soluble in the nerve endings (Fonnum, 1968;Ptrez de la Mora et al, 1973), its direct visualization with the use of antibodies has shown that it is associated with synaptosomal membrane structures (Wood et al, 1976).…”

Section: Kinetic Experimentsmentioning

confidence: 99%

Brain Glutamate Decarboxylase: Properties of Its Calcium‐Dependent Binding to Liposomes and Kinetics of the Bound and the Free Enzyme

Covarrubias

Tapia

1980

Journal of Neurochemistry

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We have postulated that brain glutamate decarboxylase (GAD; L-glutamate-1-carboxylyase, EC 4.1.1.15) plays an important role in the regulation of CNS excitability through the coupling of the synthesis and the release of GABA (Tapia, 1974;1975;Tapia et al., 1975). Because this coupling must be a membrane phenomenon, the possibility that some form of GAD may bind to membranes is particularly relevant to this hypothesis. In a previous communi-cation (Covarrubias and Tapia, 1978) we have shown that GAD present in a soluble preparation of brain tissue binds to phosphatidylcholinephosphatidylserine multilamellar liposomes in a Ca2+-dependent manner. The binding seems to be specific for GAD and does not occur with phosphatidylcholine liposomes lacking phosphatidylserine. The usefulness of this type of phospholipid vesicles as an experimental model for

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Section: Kinetic Experimentsmentioning

confidence: 99%

Brain Glutamate Decarboxylase: Properties of Its Calcium‐Dependent Binding to Liposomes and Kinetics of the Bound and the Free Enzyme

Covarrubias

Tapia

1980

Journal of Neurochemistry

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“…In skeletal muscle it is partly complexed with myosin (Currie & Webster, 1962; Byrnes & Suelter, 1965;Zydowo et al, 1974;Ashby & Frieden, 1977). The association of some other enzymes with either natural membranes (Entman et al, 1977) or with artificial phospholipid vesicles (Wooster & Wrigglesworth, 1976) has been shown to influence the catalytic properties of the enzyme. Adenylate deaminase from the heart has been little investigated so far (e.g.…”

mentioning

confidence: 99%

Modification by liposomes of the adenosine triphosphate-activating effect on adenylate deaminase from pig heart

Purzycka-Preis¹,

Prus²,

Woźniak³

et al. 1978

Biochemical Journal

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Adenylate deaminase (AMP deaminase, EC 3.5.4.6) of a high substrate specificity was purified from pig heart by chromatography on cellulose phosphate. The enzyme shows a co-operative binding of AMP [h (Hill coefficient) 2.35, with SO.5 (half-saturating substrate concentration) 5mM]. ATP and ADP act as positive effectors, lowering h to 1.55 and SO.5 to 1 mM. The addition of liposomes (phospholipid bilayers) to ATP-activated or ADP-activated enzyme causes a further shift of the h value to 1.04 and SO.5 to 0.5 mM. For ATP-activated enzyme the addition of liposomes increases Vmax. by about 100%, and for ADP-activated enzyme by 50%. Liposomes have no effect on the kinetics of AMP deaminase in the absence of ATP and ADP, and neither do they influence the inhibitory effect of orthophosphate on heart muscle AMP deaminase. Metabolic implications of these findings are discussed.

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“…It has been found that electrically charged surfaces of such model systems (monolayers, liposomes) can adsorb the enzyme and also modify its specific activity [10][11][12]. Recently, using the measurements of changes in intrinsic fluorescence spectra and the fluorescence quenching method some rearrangements in the enzyme conformation were detected [13].…”

Section: Introductionmentioning

confidence: 99%

Fluorescent probe studies on binding of glyceraldehyde‐3‐phosphate dehydrogenase to phosphatidylinositol liposomes Further evidence for conformational changes

Michalak¹,

Gutowicz²,

Modrzycka³

1987

FEBS Letters

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Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle can be adsorbed on charged lipid bilayers by electrostatic forces. Upon binding to phosphatidylinositol liposomes the enzyme modifies its conformational state as it is shown by resonance energy transfer experiments. In the presence of 2-mercaptoethanol o-phthaldialdehyde reacts with amino groups of the protein and the covalently bound fluorophore is an acceptor of excitation energy transferred from tryptophanyl residues of the protein. The observed decrease of energy transfer efficiency upon binding to phosphatidylinositol liposomes is compared with the influence of the urea on the fluorescence spectra of the labelled protein. Significance of conformational changes of the enzyme upon adsorption on liposomes in the regulating function of cell membranes is discussed.

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Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles

Cited by 24 publications

References 18 publications

Brain Glutamate Decarboxylase: Properties of Its Calcium‐Dependent Binding to Liposomes and Kinetics of the Bound and the Free Enzyme

Brain Glutamate Decarboxylase: Properties of Its Calcium‐Dependent Binding to Liposomes and Kinetics of the Bound and the Free Enzyme

Modification by liposomes of the adenosine triphosphate-activating effect on adenylate deaminase from pig heart

Fluorescent probe studies on binding of glyceraldehyde‐3‐phosphate dehydrogenase to phosphatidylinositol liposomes Further evidence for conformational changes

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