scholarly journals Role of acyl carrier protein isoforms in plant lipid metabolism

1990 ◽  
Keyword(s):  
Lipid Metabolism ◽  
Acyl Carrier Protein ◽  
Protein Isoforms ◽  
Carrier Protein ◽  
Plant Lipid

The role of acyl carrier protein isoforms from Cuphea lanceolata seeds in the de-novo biosynthesis of medium-chain fatty acids

Planta ◽  
1998 ◽  
Vol 205 (2) ◽  
pp. 263-268 ◽  
Author(s):  
Burkhardt Siegfried Schütt ◽  
Monika Brummel ◽  
Ricardo Schuch ◽  
Friedrich Spener
Keyword(s):  
Fatty Acids ◽  
De Novo ◽  
Acyl Carrier Protein ◽  
Protein Isoforms ◽  
Carrier Protein ◽  
Medium Chain ◽  
Medium Chain Fatty Acids ◽  
De Novo Biosynthesis ◽  
Cuphea Lanceolata

scholarly journals Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver

1975 ◽  
Vol 146 (1) ◽  
pp. 223-229 ◽  
Author(s):  
J W Harding ◽  
E A Pyeritz ◽  
E S Copeland ◽  
H B White
Keyword(s):  
Lactate Dehydrogenase ◽  
High Fat Diet ◽  
Acyl Carrier Protein ◽  
Fatty Acid Synthetase ◽  
Carrier Protein ◽  
High Fat ◽  
Carbohydrate Diet ◽  
Metabolic Role ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The metabolic role of hepatic NAD-linked glycerol 3-phosphate dehydrogenase (EC 1.1.1.8) was investigated vis-a-vis glyceride synthesis, glyceride degradation and the maintainence of the NAD redox state. 2. Five-week-old chickens were placed on five dietary regimes: a control group, a group on an increased-carbohydrate-lowered-fat diet, a group on a high-fat-lowered-carbohydrate diet, a starved group and a starved-refed group. In each group the specific activity (mumol/min per g wet wt. of tissue) of hepatic glycerol 3-phosphate dehydrogenase was compared with the activities of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, glycerol kinase (EC 2.7.1.30) and lactate dehydrogenase (EC 1.1.1.27). 3. During starvation, the activities of glycerol 3-phosphate dehydrogenase, glycerol kinase and lactate dehydrogenase rose significantly. After re-feeding these activities returned to near normal. All three activities rose slightly on the high-fat diet. Lactate dehydrogenase activity rose slightly, whereas those of the other two enzymes fell slightly on the increased-carbohydrate-lowered-fat diet. 4. The activity of the β-oxoacyl-(acyl-carrier protein) reductase component of fatty acid synthetase, a lipid-synthesizing enzyme, contrasted strikingly with the other three enzyme activities. Its activity was slightly elevated on the increased-carbohydrate diet and significantly diminished on the high-fat diet and during starvation. 5. The changes in activity of the chicken liver isoenzyme of glycerol 3-phosphate dehydrogenase in response to dietary stresses suggest that the enzyme has an important metabolic role other than or in addition to glyceride biosynthesis.

The role of β-ketoacyl-acyl carrier protein synthase III in the condensation steps of fatty acid biosynthesis in sunflower

Planta ◽  
2010 ◽  
Vol 231 (6) ◽  
pp. 1277-1289 ◽  
Author(s):  
Damián González-Mellado ◽  
Penny von Wettstein-Knowles ◽  
Rafael Garcés ◽  
Enrique Martínez-Force
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Acid Biosynthesis

scholarly journals Activity of Acyl Carrier Protein Isoforms in Reactions of Plant Fatty Acid Metabolism

1986 ◽  
Vol 82 (2) ◽  
pp. 448-453 ◽  
Author(s):  
Daniel J. Guerra ◽  
John B. Ohlrogge ◽  
Margrit Frentzen
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Acyl Carrier Protein ◽  
Protein Isoforms ◽  
Carrier Protein

scholarly journals A Conserved Histidine Is Essential for Glycerolipid Acyltransferase Catalysis

1998 ◽  
Vol 180 (6) ◽  
pp. 1425-1430 ◽  
Author(s):  
Richard J. Heath ◽  
Charles O. Rock
Keyword(s):  
Aspartic Acid ◽  
Acyl Carrier Protein ◽  
Site Directed Mutagenesis ◽  
Carrier Protein ◽  
Synthetase Activity ◽  
Acyltransferase Activity ◽  
Acyl Acceptor ◽  
Aspartic Acid Residue ◽  
Membrane Bound

ABSTRACT Sequence analysis of membrane-bound glycerolipid acyltransferases revealed that proteins from the bacterial, plant, and animal kingdoms share a highly conserved domain containing invariant histidine and aspartic acid residues separated by four less conserved residues in an HX4D configuration. We investigated the role of the invariant histidine residue in acyltransferase catalysis by site-directed mutagenesis of two representative members of this family, the sn-glycerol-3-phosphate acyltransferase (PlsB) and the bifunctional 2-acyl-glycerophosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase (Aas) ofEscherichia coli. Both the PlsB[H306A] and Aas[H36A] mutants lacked acyltransferase activity. However, the Aas[H36A] mutant retained significant acyl-acyl carrier protein synthetase activity, illustrating that the lack of acyltransferase activity was specifically associated with the H36A substitution. The invariant aspartic acid residue in the HX4D pattern was also important. The substitution of aspartic acid 311 with glutamic acid in PlsB resulted in an enzyme with significantly reduced catalytic activity. Substitution of an alanine at this position eliminated acyltransferase activity; however, the PlsB[D311A] mutant protein did not assemble into the membrane, indicating that aspartic acid 311 is also important for the proper folding and membrane insertion of the acyltransferases. These data are consistent with a mechanism for glycerolipid acyltransferase catalysis where the invariant histidine functions as a general base to deprotonate the hydroxyl moiety of the acyl acceptor.

scholarly journals Mitochondrial Fatty Acid Synthase Utilizes Multiple Acyl Carrier Protein Isoforms

2020 ◽  
Vol 183 (2) ◽  
pp. 547-557
Author(s):  
Xinyu Fu ◽  
Xin Guan ◽  
Rachel Garlock ◽  
Basil J. Nikolau
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Protein Isoforms ◽  
Carrier Protein ◽  
Mitochondrial Fatty Acid
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