1.3.1.39: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

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For detailed information about enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), go to the full flat file.

Reaction

Synonyms

acyl-ACP dehydrogenase, enoyl-ACP reductase, enoyl-ACP reductase III, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, FabI, FabK, FabL, NADPH 2-enoyl Co A reductase, PG1416

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.1 With NAD⁺ or NADP⁺ as acceptor

                1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

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Results	in table
1288	AA Sequence
2	Application
1	CAS Registry Number
2	Cloned(Commentary)
6	Cofactor
2	Crystallization (Commentary)
5	IC50 Value
7	Inhibitors
3	KM Value [mM]
1	Localization
1	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
12	Organism
9	Pathway
60	PDB ID
1	pH Stability
1	Reaction
3	Reaction Type
10	Reference
5	Source Tissue
3	Storage Stability
9	Substrates and Products (Substrate)
2	Subunits
14	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 1.3.1.39 - enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

native enzyme and in complex with NADPH and inhibitor triclosan, to 2.8 A and 1.8 A resolution, respectively

Bacillus subtilis

P71079

725712

apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation

Staphylococcus aureus

Q6GI75

726455