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Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH)

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IUBMB Comments
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 . The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
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UNIPROT: Q9BJJ9
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The enzyme appears in viruses and cellular organisms
Synonyms
pfenr, enoyl-acyl carrier protein, enoyl acyl carrier protein reductase, mtinha, enoyl acp reductase, enoyl-reductase, nadh-dependent enoyl-acp reductase, fabi1, fabi2, nadh-dependent enoyl-acyl carrier protein reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cold-shock induced protein 15
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CSI15
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enoyl-ACP reductase
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NADH-dependent enoyl-ACP reductase
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NADH-enoyl acyl carrier protein reductase
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NADH-specific enoyl-ACP reductase
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reductase, enoyl-[acyl carrier protein]
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VEG241
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vegetative protein 241
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NAD+ oxidoreductase
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [3]. The FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37251-08-4
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(2-amino-4-chlorophenoxy)-5-chlorophenol
IC50 for Plasmodium falciparum in culture 0.0084 mM
3-hydroxy-4-phenoxybenzaldehyde
IC50 for Plasmodium falciparum in culture 0.077 mM
4-(2,4-dichlorophenoxy)-3-hydroxybenzaldehyde
IC50 for Plasmodium falciparum in culture 0.021 mM
triclosan
competitive with NADH, uncompetitive with NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001
2-(2-amino-4-chlorophenoxy)-5-chlorophenol
pH not specified in the publication, temperature not specified in the publication
0.00013
3-hydroxy-4-phenoxybenzaldehyde
pH not specified in the publication, temperature not specified in the publication
0.00018
4-(2,4-dichlorophenoxy)-3-hydroxybenzaldehyde
pH not specified in the publication, temperature not specified in the publication
0.000025 - 0.000028
triclosan
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
2-(2-amino-4-chlorophenoxy)-5-chlorophenol
Plasmodium falciparum
pH not specified in the publication, temperature not specified in the publication
0.00028
3-hydroxy-4-phenoxybenzaldehyde
Plasmodium falciparum
pH not specified in the publication, temperature not specified in the publication
0.00038
4-(2,4-dichlorophenoxy)-3-hydroxybenzaldehyde
Plasmodium falciparum
pH not specified in the publication, temperature not specified in the publication
0.000033 - 0.000066
triclosan
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9BJJ9_PLAFA
432
0
49827
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations of tetrameric enzyme in different states of cofactor and ligand binding. Simulations show fluctuations in the substrate-binding loop and provide data of the pocket volume
mutants A372M, K316A in cimolex with triclosan, to 2.5 and 2.05 A resolution, respectively. The enzyme has a conserved salt bridge which stabilizes the substrate binding loop and appears to be important for the active conformation
X-ray crystal structures of Plasmodium falciparum enzyme in complex with triclosan variants having different substituted and unsubstituted groups at different key functional locations. 4 and 2' substituted compounds have more interactions with the protein, cofactor, and solvents when compared with triclosan. Substitution at the 2' position of triclosan causes the relocation of a conserved water molecule, leading to an additional hydrogen bond with the inhibitor. 2' and 4' unsubstituted compounds show a movement away from the hydrophobic pocket to compensate for the interactions made by the halogen groups of triclosan
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A372M
mutation increases the affinity of the enzyme towards triclosan to almost double
A372V
mutation increases the affinity of the enzyme towards triclosan to almost double
A372V/K316A
enzymatically inactive
A372V/K316E
enzymatically inactive
D370A
enzymatically inactive
D370K
enzymatically inactive
K316A
no change in affinity to triclosan
K316E
enzymatically inactive
K316I
enzymatically inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maity, K.; Bhargav, S.P.; Sankaran, B.; Surolia, N.; Surolia, A.; Suguna, K.
X-ray crystallographic analysis of the complexes of enoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition
IUBMB Life
62
467-476
2010
Plasmodium falciparum (Q9BJJ9), Plasmodium falciparum
Manually annotated by BRENDA team
Maity, K.; Banerjee, T.; Prabakaran, N.; Surolia, N.; Surolia, A.; Suguna, K.
Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from Plasmodium falciparum
IUBMB Life
63
30-41
2011
Plasmodium falciparum (Q9BJJ9), Plasmodium falciparum
Manually annotated by BRENDA team
Lindert, S.; McCammon, J.A.
Dynamics of Plasmodium falciparum enoyl-ACP reductase and implications on drug discovery
Protein Sci.
21
1734-1745
2012
Plasmodium falciparum (Q9BJJ9), Plasmodium falciparum
Manually annotated by BRENDA team