Interaction of D-beta-hydroxybutyrate apodehydrogenase with phospholipids.

Gazzotti, Paolo; Bock, Hans-Georg O.; Fleischer, Sidney

doi:10.1016/s0021-9258(19)41122-8

Cited by 115 publications

(38 citation statements)

References 27 publications

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“…One clearcut case has been described in the literature where lipid activation of a membrane enzyme is correlated with altered cofactor binding. This is 0-hydroxybutyrate dehydrogenase from liver, which is activated specifically by phosphatidylcholine (Gazzotti et al, 1975;Grover et al, 1975;Houslay et al, 1975). The changes in the binding isotherm of NADH in the presence of the phospholipid are much less subtle than those reported in this work; no binding of NADH to 0-hydroxybutyrate dehydrogenase could be detected in the absence of the lipid activator (Gazzotti et al, 1974).…”

Section: Discussioncontrasting

confidence: 49%

Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase

O'Brien¹,

Blake²,

Gennis³

1977

Biochemistry

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Section: Discussioncontrasting

confidence: 49%

Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase

O'Brien¹,

Blake²,

Gennis³

1977

Biochemistry

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“…Unlike other enzymes such as D-0-hydroxy butyrate dehydrogenase (Grover et al, 1975;Gazzotti et al, 1975) where choline is required for activity of the pure enzyme, pure alkaline phosphatase activity was neither lost upon treatment with phospholipase D nor were lecithins required for activity (Table IV). The absence of any role of inositol or choline in the insertion of rat intestinal alkaline phosphatase is interesting, since such a role for inositol phosphate has been suggested for kidney and liver enzyme from rabbit (Low & Finean 1977a;Yusufi et al, 1983) and kidney enzyme from dog (Low & Zilversmit, 1980).…”

Section: Discussionmentioning

confidence: 98%

Membrane interactions of rat intestinal alkaline phosphatase: role of polar head groups

1985

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Lipid-protein interactions with purified membranous intestinal alkaline phosphatase have been studied by using rat intestine. The enzyme was incorporated equally well into neutral lecithin and anionic liposomes, including those made from phosphatidic acid alone. It could not be solubilized with chaotropic salts nor by phospholipases C and D from either native membranes or phospholipid vesicles. Detergents effected nearly complete release of enzyme from the vesicles. Phosphatase activity was lost upon treatment with phospholipase D alone. The activity was restored with free choline, or choline containing phospholipids, but not by the addition of other phospholipids or amines. The catalytic activity was also lower when the enzyme was bound to a phosphatidylcholine vesicle containing additional phosphatidic acid. Neither phosphatidylserine nor phosphatidylinositol addition altered enzyme activity. These results show that the enzyme binds to the membrane by a primary hydrophobic interaction with membrane phospholipids without requiring the polar head group and that the enzyme activity is affected via a secondary interaction with choline. We suggest that choline protects the active site of brush border alkaline phosphatase from inhibition by endogenous membrane phosphate groups.

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“…The apo-BDH used in these studies was purified to homogeneity as described by Fleischer (1974, 1975) and was stored frozen in a liquid nitrogen refrigerator. The lipids were prepared as described previously (Gazzotti et al, 1975), except that PC(8:0) was stored at -20 °C as a 1 mM stock solution in water and was maintained at 40 °C for the studies described below. [14C]PC(8:0), synthesized from [l-14C]octanoic acid as described previously (Gazzotti et al, 1975), was used, after dilution with unlabeled PC(8:0), for measurement of the concentration of unbound PC(8:0) in the presence of BDH (see below).…”

mentioning

confidence: 99%

“…The lipids were prepared as described previously (Gazzotti et al, 1975), except that PC(8:0) was stored at -20 °C as a 1 mM stock solution in water and was maintained at 40 °C for the studies described below. [14C]PC(8:0), synthesized from [l-14C]octanoic acid as described previously (Gazzotti et al, 1975), was used, after dilution with unlabeled PC(8:0), for measurement of the concentration of unbound PC(8:0) in the presence of BDH (see below). Protein was determined by the procedure of Lowry et al (1951) with a BSA standard.…”

mentioning

confidence: 99%

“…Thus, if 1 g of PC(8:0) was bound/g of apo-BDH, ' would equal 0.732 as compared to 0.735, which is the partial specific volume of apo-BDH. The amount of PC(8:0) bound to the apo-BDH was estimated by Gazzotti et al (1975) to be about 10 mol/mol of subunit (0.17 g/g of apo-BDH), using equilibrium binding with gel-exclusion chromatography. Therefore, the contribution of the lipid to the effective partial specific volume of the BDH-PC(8:0) complex in the buffer solution used is considered negligible for purposes of the calculations.…”

mentioning

confidence: 99%

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Hydrodynamic properties of D-β-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme

Jo¹,

La²,

Smigel³

et al. 1978

Biochemistry

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The hydrodynamic properties of purified D-ßhydroxybutyrate dehydrogenase (BDH), a lecithin-requiring enzyme isolated from bovine heart mitochondria, have been studied using the active-enzyme sedimentation technique. An active complex of BDH with dioctanoyl-L-a-phosphatidylcholine, PC(8:0), was sedimented under assay conditions, and the sedimenting boundary was followed by observing the reduction of NAD+. Between 2.4 and 30 µg of BDH/mL, the ¿ 2o,w increased and was inversely related to the enzymatic activity. The most active species has the smallest apparent s2o,w (3.3 ± 0.2 S). The diffusion coefficient of the BDH-PC(8:0) complex at 2.4 jug/mL, measured by the free diffusion method, was found to be 4.9 ± 0.5 X 10-7 cm2/s; at higher protein concentrations, Z)2o,w decreased. The hydrodynamic studies both of the active BDH-PC(8:0) complex and of the apoen-^Biological membranes are macromolecular complexes consisting of proteins and phospholipids. D-/3-Hydroxybutyrate dehydrogenase, normally bound to the mitochondrial inner membrane, has been purified from bovine heart mitochondria to homogeneity as a soluble, phospholipid-free protein, apo-

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Interaction of D-beta-hydroxybutyrate apodehydrogenase with phospholipids.

Cited by 115 publications

References 27 publications

Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase

Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase

Membrane interactions of rat intestinal alkaline phosphatase: role of polar head groups

Hydrodynamic properties of D-β-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme

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