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Information on EC 1.3.1.104 - enoyl-[acyl-carrier-protein] reductase (NADPH) Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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enoyl-[acyl-carrier-protein] reductase (NADPH)
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an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
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fatty acid elongation -- saturated
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Fatty acid biosynthesis
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acyl-[acyl-carrier protein]:NADP+ oxidoreductase
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
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enoyl-ACP reductase
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enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase
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NADPH 2-enoyl Co A reductase
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FabL
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gene name
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YgaA
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UniProt
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UniProt
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Uniprot
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physiological function
expression complements the Escherichia coli fabI temperature-sensitive mutant
physiological function
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expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type
physiological function
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expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type
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crotonyl-N-acetylcysteamine + NADPH + H+
butyryl-N-acetylcysteamine + NADP+
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trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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additional information
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no cofactor: NADH
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NADPH
exhibits specific and positive cooperative binding of NADPH. The cofactor concentration that yields 50% of the maximal rate is 65 microM
NADPH
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enzyme does not exhibit cooperative binding of NADPH
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triclosan
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enzyme is reversibly inhibited by triclosan, but does not form a stable ternary complex
triclosan
the introduction of a plasmid expressing the enzyme gene leads to triclosan resistance
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8
crotonyl-N-acetylcysteamine
pH 7.5, 25°C
0.016
NADPH
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pH 7.5, 25°C
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0.003
triclosan
Staphylococcus aureus
Q9RMI3
pH 7.5, 25°C
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Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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27100
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x * 27100, calculated
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x * 27100, calculated
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x * 27100, calculated
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both free form and complexed with NADP+ and inhibitor triclosan, to 2.2 and 1.8 A resolution, respectively. The substrate-binding region in the apo-FabL structure is found in the open form. In addition, the beta4-alpha5 and beta5-alpha7 regions, which include the catalytic residues as well as the cofactor binding residues, get collapsed into the pocket. These differences result in a tetrameric arrangement totally different from NADH-dependent isoform FabI
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to 2.5 A resolution. Hexagonal space group P622, with unit-cell parameters a = b = 139.56, c = 62.75 A , alpha = beta = 90, gamma = 120°
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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G23S
mutation increases the resistance of Staphylococcus aureus to triclosan by an order of magnitude
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ETR1_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
376
41439
Swiss-Prot
ETR1_CANGA
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
385
42620
Swiss-Prot
ETR1_CANTR
386
42161
Swiss-Prot
ETR1_DEBHA
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
378
41163
Swiss-Prot
ETR1_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
382
42256
Swiss-Prot
ETR1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
372
41230
Swiss-Prot
ETR1_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
376
41206
Swiss-Prot
ETR1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
380
42067
Swiss-Prot
ETR2_CANTR
386
42117
Swiss-Prot
ETR2_DEBHA
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
387
42554
Swiss-Prot
FABL_BACSU
Bacillus subtilis (strain 168)
250
27178
Swiss-Prot
MECR_XENTR
350
38669
Swiss-Prot
MECR1_CAEEL
344
38195
Swiss-Prot
MECR2_CAEEL
346
37944
Swiss-Prot
MECR_ARATH
375
40823
Swiss-Prot
MECR_BOVIN
373
40275
Swiss-Prot
MECR_DANRE
377
41079
Swiss-Prot
MECR_DICDI
350
38735
Swiss-Prot
MECR_DROME
357
39111
Swiss-Prot
MECR_HUMAN
373
40462
Swiss-Prot
MECR_MOUSE
373
40343
Swiss-Prot
MECR_RAT
373
40327
Swiss-Prot
A0A1B9ELT7_9ACTN
270
28897
TrEMBL
A0A1A9GH38_9ACTN
244
24448
TrEMBL
A0A178XFT5_9PSEU
249
25188
TrEMBL
A0A0J6YQF5_9MYCO
238
24536
TrEMBL
A0A083ZWE7_9GAMM
250
27798
TrEMBL
A0A0F0KCT0_9MICO
254
26651
TrEMBL
A0A0M2HI33_9MICO
254
26559
TrEMBL
A0A1V5U9R3_9BACT
259
28095
TrEMBL
A0A1D2I9R8_9ACTN
271
28503
TrEMBL
A0A1V5L3A5_9ACTN
234
25020
TrEMBL
A0A0F0K9T4_9MICO
254
26559
TrEMBL
A0A1U9ISZ4_HELPX
262
28548
TrEMBL
A0A178WSK1_9PSEU
261
27372
TrEMBL
A0A0K6K7P2_BACCE
250
27182
TrEMBL
A0A0G3XU10_9BACI
249
26487
TrEMBL
A0A0Q0V4R2_9BACI
249
26528
TrEMBL
A0A1Q9B6A8_BACPU
250
27344
TrEMBL
A0A0J6V9Z2_9MYCO
242
25290
TrEMBL
A0A1Y5TTA9_9PROT
250
26057
TrEMBL
A0A098G835_9GAMM
251
26905
TrEMBL
A0A1V6I245_9BACT
260
29137
TrEMBL
A0A124C084_9ACTN
1844
195323
TrEMBL
A0A1Q2Z9W1_9ACTN
272
29412
TrEMBL
A0A075QXJ0_BRELA
252
27272
TrEMBL
A0A1V5SNJ3_9BACT
252
26866
TrEMBL
A0A0F0KDF4_9MICO
254
26931
TrEMBL
A0A1T5I097_9GAMM
256
27508
TrEMBL
A0A1U7CSQ0_9BACT
256
27004
TrEMBL
A0A0F2CDX7_9MICO
254
26608
TrEMBL
A0A1Q2Z1Z8_9ACTN
1852
193047
TrEMBL
A0A0N0RG05_9CHLR
254
27506
TrEMBL
A0A117E5L6_9ACTN
252
26744
TrEMBL
A0A0J6VVI6_9MYCO
242
25307
TrEMBL
A0A0F0L8U4_9MICO
254
26657
TrEMBL
A0A1V5XKV2_9DELT
271
29622
TrEMBL
A0A1C0AUY6_9PROT
259
28239
TrEMBL
A0A1V5PAY0_9CHLR
269
28182
TrEMBL
A0A1V5LI77_9BACT
219
23423
TrEMBL
A0A0X8X2B0_9SPHI
280
30412
TrEMBL
A0A0M2H1S8_9MICO
254
26359
TrEMBL
A0A1W6KA79_9ALTE
257
27400
TrEMBL
A0A1X6ZG53_9RHOB
218
22978
TrEMBL
A0A1C0B1K7_9PROT
259
28239
TrEMBL
A0A0N0Z3D5_9BACI
249
26499
TrEMBL
A0A178X5W0_9PSEU
251
26343
TrEMBL
A0A0M2GZN8_9MICO
257
27059
TrEMBL
A0A100J0A8_9ACTN
1859
193813
TrEMBL
A0A1C3IFY3_9VIBR
227
24063
TrEMBL
A0A0R0LK38_9PROT
260
28613
TrEMBL
A0A0D1EH53_9RHOB
288
29927
TrEMBL
A0A0F0LRN5_9MICO
257
26612
TrEMBL
A0A0M2WS65_9BURK
262
27571
TrEMBL
A0A1V5CF80_9DELT
244
25940
TrEMBL
A0A1V5RE39_9BACT
252
26833
TrEMBL
A0A1L8QM71_PSEAH
251
26648
TrEMBL
A0A1V2MZQ5_9ACTN
252
26802
TrEMBL
A0A0U5BN88_9BACL
195
21228
TrEMBL
A0A1V5THS4_9BACT
278
30004
TrEMBL
A0A0Q2JSL6_CAMCO
259
28164
TrEMBL
A0A1F2PS52_RHOER
279
29258
TrEMBL
A0A1V5RX09_9CHLR
259
27569
TrEMBL
A0A1Y0HKM3_9PROT
255
27428
TrEMBL
A0A0F0LVT9_9MICO
251
26463
TrEMBL
A0A1V6HC09_9BACT
262
27297
TrEMBL
A0A1W7BBM9_OXAFO
262
28337
TrEMBL
A0A1V5LJK1_9BACT
276
29515
TrEMBL
A0A1V5RX01_9CHLR
270
28376
TrEMBL
A0A1Q9NBP8_9ARCH
253
27792
TrEMBL
A0A1Y2NLH4_STRPT
271
27471
TrEMBL
A0A0F0LGK6_9MICO
254
26990
TrEMBL
A0A100J4X4_9ACTN
272
29411
TrEMBL
A0A0U5B8G0_9BACL
44
4848
TrEMBL
A0A150HCH2_9MICO
254
26329
TrEMBL
A0A1V5SGD4_9BACT
252
26721
TrEMBL
A0A0N9YA57_9ARCH
262
28571
TrEMBL
A0A1C0B5F1_9PROT
259
28266
TrEMBL
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Heath, R.J.; Li, J.; Roland, G.E.; Rock, C.O.
Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene
J. Biol. Chem.
275
4654-4659
2000
Staphylococcus aureus (Q9RMI3)
brenda
Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis
J. Biol. Chem.
275
40128-40133
2000
Bacillus subtilis (P71079), Bacillus subtilis 168 (P71079)
brenda
Kim, K.H.; Park, J.K.; Ha, B.H.; Moon, J.H.; Kim, E.E.
Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis
Acta Crystallogr. Sect. F
63
246-248
2007
Bacillus subtilis 168 (P71079), Bacillus subtilis (P71079)
brenda
Kim, K.H.; Ha, B.H.; Kim, S.J.; Hong, S.K.; Hwang, K.Y.; Kim, E.E.
Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis
J. Mol. Biol.
406
403-415
2011
Bacillus subtilis 168 (P71079), Bacillus subtilis (P71079)
brenda
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