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2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
a fatty acyl-CoA + 2 NADPH + 2 H+
a fatty aldehyde + CoA + 2 NADP+
Substrates: -
Products: -
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
Substrates: -
Products: -
r
arachidonoyl-CoA + NADPH + H+
arachidonic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 86% activity compared to hexadecanoyl-CoA
Products: -
?
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
Substrates: -
Products: -
r
cis-11-hexadecenal + CoA + NADP+
(E)-hexadec-11-enoyl-CoA + NADPh + H+
Marinobacter nauticus
-
Substrates: -
Products: -
?
decanoyl-CoA + NAD(P)H
decanal + NAD(P)+
-
Substrates: 2.5% of activity with tetradecanoyl-CoA
Products: -
?
docosanoyl-CoA + NADPH
docosanal + NADP+
dodecanoyl-CoA + NAD(P)H
dodecanal + NAD(P)+
-
Substrates: 33% of activity with tetradecanoyl-CoA
Products: -
?
dodecanoyl-CoA + NADPH + H+
dodecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 26% activity compared to hexadecanoyl-CoA
Products: -
?
eicosanoyl-CoA + NAD(P)H
eicosanal + NAD(P)+
-
Substrates: 2.5% of activity with tetradecanoyl-CoA
Products: -
?
eicosanoyl-CoA + NADPH
eicosanal + NADP+
heptadecanoyl-CoA + NADPH + H+
heptadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
hexadecanal + CoA + NAD+
hexadecanoyl-CoA + NADH + H+
Substrates: -
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
hexadecanoyl-CoA + NADH
hexadecanal + NAD+ + CoA
-
Substrates: reduction of NAD+ is at most 5% of the rate of NADH oxidoreduction, the enzyme is primarily a reductase and not an aldehyde dehydrogenase
Products: -
?
hexadecanoyl-CoA + NADH + H+
hexadecanal + CoA + NAD+
-
Substrates: -
Products: -
r
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
octadecanoyl-CoA + NAD(P)H
octadecanal + NAD(P)+
-
Substrates: 44% of activity with tetradecanoyl-CoA
Products: -
?
octadecanoyl-CoA + NADH
octadecanal + NAD+ + CoA
-
Substrates: slowly, octadecanoyl-CoA is identical with stearoyl-CoA
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
octanoyl-CoA + NADPH + H+
octanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 9% activity compared to hexadecanoyl-CoA
Products: -
?
oleoyl-CoA + NADPH + H+
oleic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 78% activity compared to hexadecanoyl-CoA
Products: -
?
palmitoleoyl-CoA + NADPH + H+
palmitoleic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 99% activity compared to hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NAD(P)H
tetradecanal + NAD(P)+
-
Substrates: -
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
[hexadecanoyl]-acyl carrier protein + NADPH + H+
?
-
Substrates: preferred substrate
Products: -
?
additional information
?
-
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
docosanoyl-CoA + NADPH
docosanal + NADP+
-
Substrates: 12.7% of activity with hexadecanoyl-CoA
Products: -
?
docosanoyl-CoA + NADPH
docosanal + NADP+
-
Substrates: 12.7% of activity with hexadecanoyl-CoA
Products: -
?
eicosanoyl-CoA + NADPH
eicosanal + NADP+
-
Substrates: 7.8% of activity with hexadecanoyl-CoA
Products: -
?
eicosanoyl-CoA + NADPH
eicosanal + NADP+
-
Substrates: 7.8% of activity with hexadecanoyl-CoA
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
-
Substrates: 90% of activity with tetradecanoyl-CoA
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
-
Substrates: NADH gives almost 60% of the activity obtained with NADPH, after palmitoyl-CoA affinity column purification enzyme is absolutely dependent on NADPH as cofactor
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NAD(P)H
hexadecanal + NAD(P)+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 100% activity
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Substrates: highest activity
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: 24% conversion efficiency
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
-
Substrates: 77.2% of activity with hexadecanoyl-CoA
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
-
Substrates: 77.2% of activity with hexadecanoyl-CoA
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Substrates: -
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
-
Substrates: low activity
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 69% activity compared to hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
Substrates: 65.1% of activity with hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
Substrates: 65.1% of activity with hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
Substrates: -
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
Substrates: preferred substrate, 34% conversion efficiency
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 60% activity compared to hexadecanoyl-CoA
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
additional information
?
-
-
Substrates: no products are detected when using C18:1-CoA, 2-methyl-16:0-CoA, 2-methyl-18:0-CoA or C16:0 free fatty acid as substrates
Products: -
?
additional information
?
-
Substrates: Arabidopsis thaliana AtFAR2 has the ability to use both, C16:0-ACP and C16:0-CoA substrates for the production of C16:0- alcohol, purified enzyme AtFAR2 is specific for acyl-ACP substrates, AtFAR2 shows the highest activity towards C16:0-CoA, approximately 11times higher in comparison to the activity towards C18:0-CoA. AtFAR2 displays a very low activity with C18:1-CoA, and application of C14:0-CoA as a substrate generates only aldehyde and free fatty acid
Products: -
?
additional information
?
-
-
Substrates: Arabidopsis thaliana AtFAR2 has the ability to use both, C16:0-ACP and C16:0-CoA substrates for the production of C16:0- alcohol, purified enzyme AtFAR2 is specific for acyl-ACP substrates, AtFAR2 shows the highest activity towards C16:0-CoA, approximately 11times higher in comparison to the activity towards C18:0-CoA. AtFAR2 displays a very low activity with C18:1-CoA, and application of C14:0-CoA as a substrate generates only aldehyde and free fatty acid
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
additional information
?
-
Marinobacter nauticus
-
Substrates: the enzyme exhibits no detectable reduction with free fatty acids, less than 1% activity with acetaldehyde and propanal
Products: -
?
additional information
?
-
-
Substrates: substrate chain length specificity of the enzyme is C2-C12, highest activity with C12 substrate, overview. The overall activity of the enzyme is low compared to other PduP enzymes
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
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2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
a fatty acyl-CoA + 2 NADPH + 2 H+
a fatty aldehyde + CoA + 2 NADP+
Substrates: -
Products: -
?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
-
Substrates: -
Products: -
r
arachidonoyl-CoA + NADPH + H+
arachidonic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 86% activity compared to hexadecanoyl-CoA
Products: -
?
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
-
Substrates: -
Products: -
r
cis-11-hexadecenal + CoA + NADP+
(E)-hexadec-11-enoyl-CoA + NADPh + H+
Marinobacter nauticus
-
Substrates: -
Products: -
?
dodecanoyl-CoA + NADPH + H+
dodecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 26% activity compared to hexadecanoyl-CoA
Products: -
?
heptadecanoyl-CoA + NADPH + H+
heptadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
hexadecanal + CoA + NAD+
hexadecanoyl-CoA + NADH + H+
Substrates: -
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
octanoyl-CoA + NADPH + H+
octanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 9% activity compared to hexadecanoyl-CoA
Products: -
?
oleoyl-CoA + NADPH + H+
oleic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 78% activity compared to hexadecanoyl-CoA
Products: -
?
palmitoleoyl-CoA + NADPH + H+
palmitoleic aldehyde + CoA + NADP+
Marinobacter nauticus
-
Substrates: 99% activity compared to hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
[hexadecanoyl]-acyl carrier protein + NADPH + H+
?
-
Substrates: preferred substrate
Products: -
?
additional information
?
-
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
2-methyl-1-hexadecanoyl-CoA + NADPH + H+
2-methyl-1-hexadecanal + CoA + NADP+
-
Substrates: -
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 100% activity
Products: -
?
hexadecanoyl-CoA + NADPH + H+
1-hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: preferred substrate
Products: -
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
Substrates: 24% conversion efficiency
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
-
Substrates: low activity
Products: -
?
octadecanoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 69% activity compared to hexadecanoyl-CoA
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
Substrates: preferred substrate, 34% conversion efficiency
Products: -
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
Marinobacter nauticus
-
Substrates: 60% activity compared to hexadecanoyl-CoA
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
additional information
?
-
-
Substrates: no products are detected when using C18:1-CoA, 2-methyl-16:0-CoA, 2-methyl-18:0-CoA or C16:0 free fatty acid as substrates
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
additional information
?
-
Marinobacter nauticus
-
Substrates: the enzyme exhibits no detectable reduction with free fatty acids, less than 1% activity with acetaldehyde and propanal
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly active with hexadecanoyl-CoA and shows lower activity with tetradecanoyl-CoA or octadecanoyl-CoA
Products: -
?
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Johnson, R.C.; Gilbertson, J.R.
Isolation, characterization, and partial purification of a fatty acyl coenzyme A reductase from bovine cardiac muscle
J. Biol. Chem.
247
6991-6998
1972
Bos taurus
brenda
Wang, X.; Kolattukudy, P.E.
Solubilization, purification and characterization of fatty acyl-CoA reductase from duck uropygial gland
Biochem. Biophys. Res. Commun.
208
210-215
1995
Anas platyrhynchos
brenda
Lee, C.Y.; Meighen, E.A.
Cysteine-286 as the site of acylation of the lux-specific fatty acyl-CoA reductase
Biochim. Biophys. Acta
1338
215-222
1997
Photobacterium leiognathi, Photobacterium phosphoreum
brenda
Vioque, J.; Kolattukudy, P.E.
Resolution and purification of an aldehyde-generating and an alcohol-generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.)
Arch. Biochem. Biophys.
340
64-72
1997
Pisum sativum
brenda
Reiser, S.; Somerville, C.
Isolation of mutants of Acinetobacter calcoceticus deficient in wax ester synthesis and complementation of one mutation with a gene encoding a fatty acyl coenzyme A reductase
J. Bacteriol.
179
2969-2975
1997
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus BD413
brenda
Ishige, T.; Tani, a.; Takabe, K.; Kawasaki, K.; Sakai, Y.; Kato, N.
Wax ester production from n-alkanes by Acinetobacter sp. strain M-1: ultrastructure of cellular inclusions and role of acyl coenzyme A reductase
Appl. Environ. Microbiol.
68
1192-1195
2002
Acinetobacter
brenda
Metz, J.G.; Pollard, M.R.; Anderson, L.; Hayes, T.R.; Lassner, M.W.
Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed
Plant Physiol.
122
635-644
2000
Simmondsia chinensis
brenda
Doan, T.T.; Carlsson, A.S.; Hamberg, M.; Buelow, L.; Stymne, S.; Olsson, P.
Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli
J. Plant Physiol.
166
787-796
2009
Arabidopsis thaliana (B9TSP7), Arabidopsis thaliana (Q08891), Arabidopsis thaliana (Q39152)
brenda
Teerawanichpan, P.; Qiu, X.
Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters
Lipids
45
263-273
2010
Euglena gracilis
brenda
Willis, R.M.; Wahlen, B.D.; Seefeldt, L.C.; Barney, B.M.
Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: a bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol
Biochemistry
50
10550-10558
2011
Marinobacter nauticus
brenda
Doan, T.T.; Domergue, F.; Fournier, A.E.; Vishwanath, S.J.; Rowland, O.; Moreau, P.; Wood, C.C.; Carlsson, A.S.; Hamberg, M.; Hofvander, P.
Biochemical characterization of a chloroplast localized fatty acid reductase from Arabidopsis thaliana
Biochim. Biophys. Acta
1821
1244-1255
2012
Arabidopsis thaliana
brenda
Hellenbrand, J.; Biester, E.M.; Gruber, J.; Hamberg, M.; Frentzen, M.
Fatty acyl-CoA reductases of birds
BMC Biochem.
12
64
2011
Anser anser, Gallus gallus, Tyto alba
brenda
Doan, T.T.; Carlsson, A.S.; Stymne, S.; Hofvander, P.
Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols
Acta Biochim. Pol.
63
565-570
2016
Arabidopsis thaliana (Q08891), Arabidopsis thaliana
brenda
Lan, E.; Ro, S.; Liao, J.
Oxygen-tolerant coenzyme A-acylating aldehyde dehydrogenase facilitates efficient photosynthetic n-butanol biosynthesis in cyanobacteria
Energy Environ. Sci.
6
2672-2681
2013
Porphyromonas gingivalis
-
brenda
Lehtinen, T.; Efimova, E.; Santala, S.; Santala, V.
Improved fatty aldehyde and wax ester production by overexpression of fatty acyl-CoA reductases
Microb. Cell Fact.
17
19
2018
Acinetobacter baylyi (Q6F7B8)
brenda