Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesis acyl carrier proteins

2009 ◽  
Vol 5 (6) ◽  
pp. 651 ◽  
Author(s):  
Ashish Misra ◽  
Namita Surolia ◽  
Avadhesha Surolia
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Transferase Activity ◽  
Type Ii ◽  
Carrier Proteins ◽  
Acid Biosynthesis ◽  
Acyl Carrier Proteins

scholarly journals In VivoFunctional Analyses of the Type II Acyl Carrier Proteins of Fatty Acid Biosynthesis

2007 ◽  
Vol 282 (28) ◽  
pp. 20319-20328 ◽  
Author(s):  
Nicholas R. De Lay ◽  
John E. Cronan
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Type Ii ◽  
Carrier Proteins ◽  
Acid Biosynthesis ◽  
Acyl Carrier Proteins

scholarly journals In vivo pools of free and acylated acyl carrier proteins in spinach. Evidence for sites of regulation of fatty acid biosynthesis

1991 ◽  
Vol 266 (3) ◽  
pp. 1858-1865 ◽  
Author(s):  
D Post-Beittenmiller ◽  
J G Jaworski ◽  
J B Ohlrogge
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Carrier Proteins ◽  
Acid Biosynthesis ◽  
Acyl Carrier Proteins

Combination of type II fatty acid biosynthesis enzymes and thiolases supports a functional β-oxidation reversal

2018 ◽  
Vol 45 ◽  
pp. 11-19 ◽  
Author(s):  
James M. Clomburg ◽  
Stephanie C. Contreras ◽  
Alexander Chou ◽  
Justin B. Siegel ◽  
Ramon Gonzalez
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Type Ii ◽  
Acid Biosynthesis

scholarly journals Crucial components of mycobacterium type II fatty acid biosynthesis (Fas-II) and their inhibitors

2014 ◽  
Vol 360 (2) ◽  
pp. 87-99 ◽  
Author(s):  
Xiangke Duan ◽  
Xiaohong Xiang ◽  
Jianping Xie
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Type Ii ◽  
Acid Biosynthesis ◽  
Fas Ii

Enhanced fatty acid biosynthesis and normal surfactant secretion in hypertrophic rat type II cells

1991 ◽  
Vol 260 (6) ◽  
pp. L577-L585 ◽  
Author(s):  
J. Rami ◽  
S. M. Sasic ◽  
S. A. Rooney
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Fatty Acid Biosynthesis ◽  
De Novo ◽  
Enzyme Activation ◽  
Type Ii Cells ◽  
Type Ii ◽  
Acid Biosynthesis ◽  
Surfactant Secretion ◽  
Phosphatidylcholine Secretion

Silica instillation causes lung surfactant accumulation as well as hyperplasia and hypertrophy of type II pneumocytes. Two populations of type II cells can be isolated from silica-treated rats: type IIA, which are similar to type II cells from normal animals and type IIB, which are larger and have a higher rate of phosphatidylcholine biosynthesis. We have compared fatty acid biosynthesis and phosphatidylcholine secretion in types IIA and IIB cells and in type II cells from control rats. The cells were isolated by elastase digestion and panning on immunoglobulin G-coated plates and fractionated into types IIA and IIB by centrifugal elutriation. Type IIB cells contained more phospholipid and had an enhanced rate of [3H]choline incorporation into phosphatidylcholine. The activity of choline-phosphate cytidylyltransferase was elevated in the type IIB cells and the extent of the increase was diminished when phosphatidylglycerol was included in the assay, suggesting that the enhanced activity was due to enzyme activation rather than protein synthesis. The basal rate of phosphatidylcholine secretion was the same in all three groups as was the response to a variety of secretagogues. Incorporation of [3H]acetate into fatty acids was elevated in type IIB cells and the activity of fatty acid synthase was eightfold greater than in control cells. These data show that de novo fatty acid biosynthesis is increased in hypertrophic type II cells and that surfactant secretion is not elevated.

scholarly journals Structural and dynamical rationale for fatty acid unsaturation inEscherichia coli

2019 ◽  
Vol 116 (14) ◽  
pp. 6775-6783 ◽  
Author(s):  
Greg J. Dodge ◽  
Ashay Patel ◽  
Kara L. Jaremko ◽  
J. Andrew McCammon ◽  
Janet L. Smith ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Active Sites ◽  
Fatty Acid Biosynthesis ◽  
Binding Pocket ◽  
Cross Linking ◽  
Substrate Selectivity ◽  
Acid Biosynthesis ◽  
Acyl Carrier Proteins ◽  
Dynamics Simulations

Fatty acid biosynthesis in α- and γ-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of sixEscherichia coliFabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization.

Mechanistic diversity and regulation of Type II fatty acid synthesis

2002 ◽  
Vol 30 (6) ◽  
pp. 1050-1055 ◽  
Author(s):  
H. Marrakchi ◽  
Y.-M. Zhang ◽  
C. O. Rock
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Unsaturated Fatty Acid ◽  
Fatty Acid Synthase ◽  
Fatty Acid Biosynthesis ◽  
Specific Interaction ◽  
Acid Synthesis ◽  
Protein Crystal ◽  
Type Ii ◽  
Acid Biosynthesis

Fatty acid biosynthesis is catalysed in most bacteria by a group of highly conserved proteins known as the Type II fatty acid synthase (FAS) system. The Type II system organization is distinct from its mammalian counterpart and offers several unique sites for selective inhibition by antibacterial agents. There has been remarkable progress in the understanding of the genetics, biochemistry and regulation of Type II FASs. One important advance is the discovery of the interaction between the fatty acid degradation regulator, FadR, and the fatty acid biosynthesis regulator, FabR, in the transcriptional control of unsaturated fatty acid synthesis in Escherichia coli. The availability of genomic sequences and high-resolution protein crystal structures has expanded our understanding of Type II FASs beyond the E. coli model system to a number of pathogens. The molecular diversity among the pathway enzymes is illustrated by the discovery of a new type of enoyl-reductase in Streptococcus pneumoniae [enoyl-acyl carrier protein (ACP) reductase II, FabK], the presence of two enoyl-reductases in Bacillus subtilis (enoyl-ACP reductases I and III, FabI and FabL), and the use of a new mechanism for unsaturated fatty acid formation in S. pneumoniae (trans-2-cis-3-enoyl-ACP isomerase, FabM). The solution structure of ACP from Mycobacterium tuberculosis revealed features common to all ACPs, but its extended C-terminal domain may reflect a specific interaction with very-long-chain intermediates.

scholarly journals Advances on Mechanism and Drug Discovery of Type-II Fatty Acid Biosynthesis Pathway

2020 ◽  
Vol 78 (12) ◽  
pp. 1383
Author(s):  
Jiashen Zhou ◽  
Lin Zhang ◽  
Liang Zhang
Keyword(s):  
Fatty Acid ◽  
Drug Discovery ◽  
Fatty Acid Biosynthesis ◽  
Type Ii ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis ◽  
Fatty Acid Biosynthesis Pathway
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