Role of Hydrophobic Partitioning in Substrate Selectivity and Turnover of theRicinuscommunisStearoyl Acyl Carrier Protein Δ9Desaturase†

Biochemistry ◽  
1999 ◽  
Vol 38 (39) ◽  
pp. 12833-12840 ◽  
Author(s):  
Jeffrey A. Haas ◽  
Brian G. Fox
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Substrate Selectivity

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 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 4′-Phosphopantetheine and long acyl chain-dependent interactions are integral to human mitochondrial acyl carrier protein function

MedChemComm ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 209-220 ◽  
Author(s):  
Jaimeen D. Majmudar ◽  
Xidong Feng ◽  
Nicholas G. Fox ◽  
Joseph F. Nabhan ◽  
Theresa Towle ◽  
...  
Keyword(s):  
Protein Function ◽  
Acyl Carrier Protein ◽  
Acyl Chain ◽  
Carrier Protein ◽  
Acyl Chains

Insights into the role of 4′-PP- and long acyl chains-dependent interactions in human ACPM function.

The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis

2008 ◽  
Vol 130 (20) ◽  
pp. 6336-6337 ◽  
Author(s):  
Hui Jiang ◽  
Ross Zirkle ◽  
James G. Metz ◽  
Lisa Braun ◽  
Leslie Richter ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Protein Domains ◽  
Carrier Protein ◽  
Acid Biosynthesis

scholarly journals Thioesterase II of Escherichia coli Plays an Important Role in 3-Hydroxydecanoic Acid Production

2004 ◽  
Vol 70 (7) ◽  
pp. 3807-3813 ◽  
Author(s):  
Zhong Zheng ◽  
Qiang Gong ◽  
Tao Liu ◽  
Ying Deng ◽  
Jin-Chun Chen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Physiological Role ◽  
Carrier Protein ◽  
E Coli ◽  
Thioesterase Ii ◽  
Abnormal Accumulation ◽  
Acyl Coenzyme A

ABSTRACT 3-Hydroxydecanoic acid (3HD) was produced in Escherichia coli by mobilizing (R)-3-hydroxydecanoyl-acyl carrier protein-coenzyme A transacylase (PhaG, encoded by the phaG gene). By employing an isogenic tesB (encoding thioesterase II)-negative knockout E. coli strain, CH01, it was found that the expressions of tesB and phaG can up-regulate each other. In addition, 3HD was synthesized from glucose or fructose by recombinant E. coli harboring phaG and tesB. This study supports the hypothesis that the physiological role of thioesterase II in E. coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A.

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