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a long-chain acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
-
-
-
-
?
a long-chain fatty acyl-CoA + NADPH + H+
a long-chain aldehyde + CoA + NADP+
AmFAR1 converts saturated fatty acids ranging from 16 to 22 carbon chains to their corresponding alcohols with the highest conversion efficiency shown on 18:0, AmFAR1 also shows some activities on ricinoleic acid, 16:1n-7 and 18:1n-9
aldehyde intermediate is immediately reduced to the corresponding alcohol
-
?
arachidonoyl-CoA + NADPH + H+
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenal into the corresponding (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraen-1-ol
-
?
arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
erucoyl-CoA + NADPH + H+
(13Z)-docos-13-enal + CoA + NADP+
Marinobacter nauticus
-
erucoyl-CoA i.e. (13Z)-docos-13-enoyl-CoA
further direct reduction of (13Z)-docos-13-enal into the corresponding (13Z)-docos-13-en-1-ol
-
?
fatty acyl-CoA + NADPH + H+
fatty aldehyde + CoA + NADP+
Marinobacter nauticus
-
-
reaction intermediate, enzyme converts fatty acyl-CoA directly into the corresponding fatty alcohol by four-electron reduction, free fatty aldehyde intermediate is not accessible
-
?
hexadecanoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
-
-
-
?
icosanoyl-CoA + NADPH + H+
icosanal + CoA + NADP+
Marinobacter nauticus
-
-
further direct reduction of icosanal into the corresponding icosan-1-ol
-
?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
lauroyl-CoA + NADPH + H+
dodecanal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of dodecanal into the corresponding dodecan-1-ol
-
?
myristoyl-CoA + NADP+
? + CoA + NADPH
myristoyl-CoA + NADPH
?
-
-
-
-
?
myristoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of tetradecanal into the corresponding tetradecan-1-ol
-
?
octanoyl-CoA + NADPH + H+
octanal + NADP+
Marinobacter nauticus
-
-
further reduction of octanal into the corresponding octan-1-ol
-
?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
palmitoleoyl-CoA + NADPH + H+
(9Z)-hexadec-9-enal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of (9Z)-hexadec-9-enal into the corresponding (9Z)-hexadec-9-en-1-ol
-
?
palmitoyl-ACP + NADPH
1-hexadecanol + acyl-carrier protein + NADP+
-
the recombinant acyl-CoA reductase from Simmondsia chinensis exhibits a specificty to palmitoyl-ACP and not palmitoyl-CoA when expressed in Escherichia coli
-
-
?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
palmitoyl-[acyl-carrier protein] + NADPH + H+
hexadecanal + [acyl-carrier protein] + NADP+
Marinobacter nauticus
-
-
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
?
ricinoleoyl-CoA + NADPH + H+
(9Z,12R)-12-hydroxyoctadec-9-enal + CoA + NADP+
Marinobacter nauticus
-
ricinoleoyl-CoA i.e. (9Z,12R)-12-hydroxyoctadec-9-enoyl-CoA
further direct reduction of (9Z,12R)-12-hydroxyoctadec-9-enal into the corresponding (9Z,12R)-octadec-9-ene-1,12-diol
-
?
stearoyl-CoA + NADP+
octadecanal + CoA + NADPH
44% of the activity with myristoyl-CoA
-
-
?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
tetraeicos-cis-15-enoyl-CoA + NADPH
tetraeicos-cis-15-en-1-ol + CoA + NADP+
-
-
-
-
?
additional information
?
-
arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
29% of the activity with NADPH
-
-
?
arachidoyl-CoA + NADP+
eicosanal + CoA + NADPH
29% of the activity with NADPH
-
-
?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
33% of the activity with myristoyl-CoA
-
-
?
lauroyl-CoA + NADP+
dodecanal + CoA + NADPH
33% of the activity with myristoyl-CoA
-
-
?
myristoyl-CoA + NADP+
? + CoA + NADPH
-
-
-
?
myristoyl-CoA + NADP+
? + CoA + NADPH
-
-
-
?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
Marinobacter nauticus
-
-
further direct reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
-
?
oleoyl-CoA + NADPH + H+
(9Z)-octadec-9-enal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
-
?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
90% of the activity with myristoyl-CoA
-
-
?
palmitoyl-CoA + NADP+
hexadecanal + CoA + NADPH
90% of the activity with myristoyl-CoA
-
-
?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
-
-
-
-
r
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Marinobacter nauticus
-
-
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of hexadecanal into the corresponding hexadecan-1-ol
-
?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
-
-
further direct reduction of octadecanal into the corresponding octadecan-1-ol
-
?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Marinobacter nauticus
-
-
further reduction of octadecanal into the corresponding octadecan-1-ol
-
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
-
-
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
-
-
-
?
tetradecanoyl-CoA + NADPH + H+
tetradecanal + CoA + NADP+
-
-
-
-
?
additional information
?
-
-
substrates with carbon chain lengths shorter thah 8 do not show any activity
-
-
?
additional information
?
-
substrates with carbon chain lengths shorter thah 8 do not show any activity
-
-
?
additional information
?
-
substrates with carbon chain lengths shorter thah 8 do not show any activity
-
-
?
additional information
?
-
no activity observed on 18:2n-6 and 18:3n-3
-
-
?
additional information
?
-
-
no activity observed on 18:2n-6 and 18:3n-3
-
-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
-
-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
-
-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
-
-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
-
-
?
additional information
?
-
catalyses the formation of a fatty alcohol from an acyl-CoA
-
-
?
additional information
?
-
-
enzyme only utilizes very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16, enzyme is capable of using NADPH and NADH as electron donors, but prefers NADPH to NADH
-
-
?
additional information
?
-
Marinobacter nauticus
-
in contrast to other prokaryotes, the enzyme performs the two reduction steps from acyl-CoA to fatty alcohol in a single step which is typical for eukaryotes
-
-
?
additional information
?
-
Marinobacter nauticus
-
no reaction product detected with NADH or free fatty acids
-
-
?
additional information
?
-
Marinobacter nauticus
-
shorter acyl chains than 16 carbon are less effectively utilized and with these substrates substantial amounts of both free fatty acids and fatty aldehyde are formed
-
-
?
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Cataract
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Cataract
Fatty Acyl-CoA Reductase 1 Deficiency.
Epilepsy
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Epilepsy
Fatty Acyl-CoA Reductase 1 Deficiency.
Intellectual Disability
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Intellectual Disability
Fatty Acyl-CoA Reductase 1 Deficiency.
long-chain acyl-protein thioester reductase deficiency
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
long-chain acyl-protein thioester reductase deficiency
A rare case of fatty acyl-CoA reductase 1 deficiency in an Indian infant manifesting rhizomelic chondrodystrophy phenotype.
long-chain acyl-protein thioester reductase deficiency
Familial Mitral Arcade, Tricuspid Dysplasia, Left Ventricular Noncompaction and Short-Chain Acyl-CoA Reductase Deficiency.
long-chain acyl-protein thioester reductase deficiency
Fatty Acyl-CoA Reductase 1 Deficiency.
Microcephaly
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Microcephaly
Fatty Acyl-CoA Reductase 1 Deficiency.
Neoplasms
Acyl-CoA reductase specificity and synthesis of wax esters in mouse preputial gland tumors.
Peroxisomal Disorders
A peroxisomal disorder of severe intellectual disability, epilepsy, and cataracts due to fatty acyl-CoA reductase 1 deficiency.
Tuberculosis
Catabolism of the Last Two Steroid Rings in Mycobacterium tuberculosis and Other Bacteria.
Zellweger Syndrome
Properties of the enzymes catalyzing the biosynthesis of lysophosphatidate and its ether analog in cultured fibroblasts from Zellweger syndrome patients and normal controls.
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116000
Marinobacter nauticus
-
SDS-PAGE, in agreement with mass calculated from amino acid sequence
140000
-
recombinant CpFAS1-R domain as maltose binding protein fusion protein, SDS-PAGE
205000 - 223000
-
reductase component of fatty acid reductase enzyme complex, gel filtration, SDS-PAGE after cross-linkage with bis(sulfosuccinimidyl)suberate
33000
x * 33000, SDS-PAGE
450000
-
fatty acid reductase enzyme complex composed of synthetase (s), reductase (r) and transferase (t), molar ratio s: r: t is 1: 1: 0.5, gel filtration
50000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
51000
theoretical value, verified by SDS-PAGE
52000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
55500
theoretical value, verified by SDS-PAGE
56200
-
x * 56200, SDS-PAGE
57000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
58000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
59200
calculated from sequence
61600
theoretical value, verified by SDS-PAGE
68400
theoretical value, verified by SDS-PAGE, heavily degraded
34000
-
x * 57000 + x * 34000 + x * 52000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
34000
-
x * 58000 + x * 34000 + x * 50000, reductase, transferase and synthetase subunit of the enzyme complex, SDS-PAGE
56000
theoretical value, verified by SDS-PAGE
56000
-
x * 56000, SDS-PAGE
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Wall, L.; Meighen, E.A.
Subunit structure of the fatty acid reductase complex from Photobacterium phosphoreum
Biochemistry
25
4315-4321
1986
Photobacterium phosphoreum
-
brenda
Riendeau, D.; Rodriguez, A.; Meighen, E.
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex
J. Biol. Chem.
257
6908-6915
1982
Photobacterium phosphoreum
brenda
Rodriguez, A.; Wall, L.; Raptis, S.; Zarkadas, C.G.; Meighen, E.
Different sites for fatty acid activation and acyl transfer by the synthetase subunit of fatty acid reductase: acylation of a cysteinyl residue
Biochim. Biophys. Acta
964
266-275
1988
Photobacterium phosphoreum
-
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
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 sp., Acinetobacter sp. (Q8RR58), Acinetobacter sp. M-1 (Q8RR58)
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
Wall, L.; Meighen, E.
Covalent reaction of cerulenin at the active site of acyl-CoA reductase of Photobacterium phosphoreum
Biochem. Cell Biol.
67
163-167
1989
Photobacterium phosphoreum
brenda
Rodriguez, A.; Wall, L.; Riendeau, D.; Meighen, E.
Fatty acid reductase from Photobacterium phosphoreum
Methods Enzymol.
133
172-182
1986
Photobacterium phosphoreum
-
brenda
Wall, L.; Rodriguez, A.; Meighen, E.
Intersubunit transfer of fatty acyl groups during fatty acid reduction
J. Biol. Chem.
261
15981-15988
1986
Photobacterium phosphoreum
brenda
Rodriguez, A.; Riendeau, D.; Meighen, E.
Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria. Properties and acyltransferase activity
J. Biol. Chem.
258
5233-5237
1983
Photobacterium phosphoreum
brenda
Riendeau, D.; Meighen, E.
Fatty acid reductase in bioluminescent bacteria. Resolution from aldehyde reductases and characterization of the aldehyde product
Can. J. Biochem.
59
440-446
1981
Photobacterium phosphoreum
brenda
Kalscheuer, R.; Stoeveken, T.; Luftmann, H.; Malkus, U.; Reichelt, R.; Steinbuechel, A.
Neutral lipid biosynthesis in engineered Escherichia coli: jojoba oil-like wax esters and fatty acid butyl esters
Appl. Environ. Microbiol.
72
1373-1379
2006
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 (Q1PEI6), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q93ZB9)
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
Zhu, G.; Shi, X.; Cai, X.
The reductase domain in a Type i fatty acid synthase from the apicomplexan Cryptosporidium parvum: Restricted substrate preference towards very long chain fatty acyl thioesters
BMC Biochem.
11
46
2010
Cryptosporidium parvum
brenda
Hofvander, P.; Doan, T.T.; Hamberg, M.
A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol
FEBS Lett.
585
3538-3543
2011
Marinobacter nauticus
brenda
Teerawanichpan, P.; Robertson, A.J.; Qiu, X.
A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols
Insect Biochem. Mol. Biol.
40
641-649
2010
Apis mellifera (D9MWM7), Apis mellifera
brenda