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InterPro: IPR014358 Enoyl-[acyl-carrier-protein] reductase (NADH)
Protein matches
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UniProtKB Matches: 1391 proteins |
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Accession
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IPR014358 Enoyl-ACP_Rdtase_NADH |
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Type
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Family |
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Signatures
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InterPro Relationships
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Parent
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IPR002347 Glucose/ribitol dehydrogenase
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Contains
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IPR016040 NAD(P)-binding domain
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GO Term annotation
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Process
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GO:0006633 fatty acid biosynthetic process
GO:0055114 oxidation reduction
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Function
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GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This entry contains enoyl-[acyl-carrier-protein] reductases (EC:1.3.1.9). They are components of the type II (dissociable) fatty acid synthase system and catalyse the terminal reaction in the fatty acid elongation cycle. They belong to the short-chain dehydrogenases/reductases (SDR) domain superfamily [1, 2, 3] and are therefore related to members of PIRSF000092-PIRSF000096, amongst others.
Most SDRs contain two subdomains. The N-terminal subdomain binds the coenzyme, and the C-terminal subdomain binds the substrate, determines the substrate specificity and contains amino acids involved in catalysis [1, 2, 3]. Despite low sequence similarity, all SDR structures display highly similar alpha/beta folding patterns with a central beta-sheet, typical of the Rossmann-fold
[3].
Crystal structures of these proteins have been extensively studied [4, 5, 6, 7, 8, 9, 10]. (This information was partially derived from the PFAM database, IPR002198)
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Structural links
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Database links
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Publications
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1.
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Jornvall H, Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D.
Short-chain dehydrogenases/reductases (SDR).
Biochemistry 34 6003-13 1995
[PubMed: 7742302]
http://dx.doi.org/10.1021/bi00018a001
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2.
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Persson B, Kallberg Y, Oppermann U, Jornvall H.
Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs).
Chem. Biol. Interact. 143-144 271-8 2003
[PubMed: 12604213]
http://dx.doi.org/10.1016/S0009-2797(02)00223-5
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3.
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Oppermann U, Filling C, Hult M, Shafqat N, Wu X, Lindh M, Shafqat J, Nordling E, Kallberg Y, Persson B, Jornvall H.
Short-chain dehydrogenases/reductases (SDR): the 2002 update.
Chem. Biol. Interact. 143-144 247-53 2003
[PubMed: 12604210]
http://dx.doi.org/10.1016/S0009-2797(02)00164-3
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4.
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Stewart MJ, Parikh S, Xiao G, Tonge PJ, Kisker C.
Structural basis and mechanism of enoyl reductase inhibition by triclosan.
J. Mol. Biol. 290 859-65 1999
[PubMed: 10398587]
http://dx.doi.org/10.1006/jmbi.1999.2907
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5.
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Miller WH, Seefeld MA, Newlander KA, Uzinskas IN, Burgess WJ, Heerding DA, Yuan CC, Head MS, Payne DJ, Rittenhouse SF, Moore TD, Pearson SC, Berry V, DeWolf WE Jr, Keller PM, Polizzi BJ, Qiu X, Janson CA, Huffman WF.
Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI).
J. Med. Chem. 45 3246-56 2002
[PubMed: 12109908]
http://dx.doi.org/10.1021/jm020050+
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6.
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Seefeld MA, Miller WH, Newlander KA, Burgess WJ, DeWolf WE Jr, Elkins PA, Head MS, Jakas DR, Janson CA, Keller PM, Manley PJ, Moore TD, Payne DJ, Pearson S, Polizzi BJ, Qiu X, Rittenhouse SF, Uzinskas IN, Wallis NG, Huffman WF.
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
J. Med. Chem. 46 1627-35 2003
[PubMed: 12699381]
http://dx.doi.org/10.1021/jm0204035
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7.
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Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS.
Molecular basis for triclosan activity involves a flipping loop in the active site.
Protein Sci. 8 2529-32 1999
[PubMed: 10595560]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=10595560&action=stream&blobtype=pdf
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8.
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Ward WH, Holdgate GA, Rowsell S, McLean EG, Pauptit RA, Clayton E, Nichols WW, Colls JG, Minshull CA, Jude DA, Mistry A, Timms D, Camble R, Hales NJ, Britton CJ, Taylor IW.
Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan.
Biochemistry 38 12514-25 1999
[PubMed: 10493822]
http://dx.doi.org/10.1021/bi9907779
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9.
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Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC.
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Science 279 98-102 1998
[PubMed: 9417034]
http://dx.doi.org/10.1126/science.279.5347.98
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10.
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Rafferty JB, Simon JW, Baldock C, Artymiuk PJ, Baker PJ, Stuitje AR, Slabas AR, Rice DW.
Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.
Structure 3 927-38 1995
[PubMed: 8535786]
http://dx.doi.org/10.1016/S0969-2126(01)00227-1
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Additional Reading
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Freundlich JS, Wang F, Tsai HC, Kuo M, Shieh HM, Anderson JW, Nkrumah LJ, Valderramos JC, Yu M, Kumar TR, Valderramos SG, Jacobs WR Jr, Schiehser GA, Jacobus DP, Fidock DA, Sacchettini JC.
X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy.
J. Biol. Chem. 282 2007 25436-44
[PubMed: 17567585]
http://dx.doi.org/10.1074/jbc.M701813200
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Lee HH, Moon J, Suh SW.
Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan.
Proteins 69 2007 691-4
[PubMed: 17879346]
http://dx.doi.org/10.1002/prot.21586
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Argyrou A, Vetting MW, Blanchard JS.
New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP.
J. Am. Chem. Soc. 129 2007 9582-3
[PubMed: 17636923]
http://dx.doi.org/10.1021/ja073160k
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Wang F, Langley R, Gulten G, Dover LG, Besra GS, Jacobs WR Jr, Sacchettini JC.
Mechanism of thioamide drug action against tuberculosis and leprosy.
J. Exp. Med. 204 2007 73-8
[PubMed: 17227913]
http://dx.doi.org/10.1084/jem.20062100
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He X, Alian A, Ortiz de Montellano PR.
Inhibition of the Mycobacterium tuberculosis enoyl acyl carrier protein reductase InhA by arylamides.
Bioorg. Med. Chem. 15 2007 6649-58
[PubMed: 17723305]
http://dx.doi.org/10.1016/j.bmc.2007.08.013
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