2.3.1.86: fatty-acyl-CoA synthase system
This is an abbreviated version!
For detailed information about fatty-acyl-CoA synthase system, go to the full flat file.
Word Map on EC 2.3.1.86
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2.3.1.86
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udp-glucuronosyltransferase
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glucuronidation
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farnesoid
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carvedilol
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extrahepatic
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acid-conjugating
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parapsilosis
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hyodeoxycholic
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4-hydroxyestrone
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analysis
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medicine
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biofuel production
- 2.3.1.86
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udp-glucuronosyltransferase
-
glucuronidation
-
farnesoid
- carvedilol
-
extrahepatic
-
acid-conjugating
- parapsilosis
-
hyodeoxycholic
- 4-hydroxyestrone
- analysis
- medicine
- biofuel production
Reaction
Synonyms
CpFas2, FAS, FAS1, fas2, fatty acid synthase, fatty-acyl-CoA synthase, yeast fatty acid synthase
ECTree
2.3.1.86 fatty-acyl-CoA synthase systemAdvanced search results
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results (Crystallization
Crystallization on EC 2.3.1.86 - fatty-acyl-CoA synthase system
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
a gamma subunit of the 2.6 megadalton FAS16-FAS26 stabilizes a rotated FAS conformation and rearranges ACP domains from equatorial to axial positions. The gamma subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The gamma subunit delineates the functional compartment within FAS
crystal structure of yeast FAS reveals that this large, macromolecular assembly functions as a six-chambered reactor for fatty acid synthesis. Each of the six chambers functions independently and has in its chamber wall all of the catalytic units required for fatty acid priming, elongation, and termination, while one substrate-shuttling component, ACP, is located inside each chamber and functions like a swinging arm. Surprisingly, however, the step at which the reactor is activated must occur before the complete assembly of the particle since the PPT domain that attaches the pantetheine arm to ACP lies outside the assembly, inaccessible to ACP that lies inside. Remarkably, the architectural complexity of the FAS particle results in the simplicity of the reaction mechanisms for fatty acid synthesis
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structure determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggest a model for substrate delivery that might apply to the other catalytic domains as well
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structure of the Saccharomyces cerevisiae FAS determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure of the yeast FAS complex shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggests a model for substrate delivery
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