| Entry |
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| Symbol |
fadD13
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| Name |
long-chain-fatty-acid---CoA ligase [EC: 6.2.1.3]
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| Pathway |
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| Module |
| M00086 | beta-Oxidation, acyl-CoA synthesis |
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| Reaction |
| R00390 | long-chain-fatty-acid:CoA ligase (AMP-forming) |
| R01280 | palmitate:CoA ligase (AMP-forming) |
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| Brite |
KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09103 Lipid metabolism
00061 Fatty acid biosynthesis
K28161 fadD13; long-chain-fatty-acid---CoA ligase
00071 Fatty acid degradation
K28161 fadD13; long-chain-fatty-acid---CoA ligase
Enzymes [BR:ko01000]
6. Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.3 long-chain-fatty-acid---CoA ligase
K28161 fadD13; long-chain-fatty-acid---CoA ligase
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| Other DBs |
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| Genes |
» show all
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| Reference |
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| Authors |
Khare G, Gupta V, Gupta RK, Gupta R, Bhat R, Tyagi AK |
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| Title |
Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Martinez Molina D, Hogbom M |
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| Title |
The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase: structural basis for housing lipid substrates longer than the enzyme. |
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| Journal |
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| LinkDB |
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