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a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+
a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+
-
Substrates: -
Products: -
?
fatty acyl-CoA + NAD(P)H + H+
fatty aldehyde + CoA + NAD(P)+
-
Substrates: CpFAS1-R can only utilize very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16 or fewer carbons
Products: since aldehydes are toxic to cells it is very likely that the fatty aldehyde is immediately transformed into the corresponding alcohol by the enzyme complex
?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl-carrier protein + NAD(P)+
-
Substrates: -
Products: -
?
hexacosanoyl-CoA + NAD(P)H + H+
hexacosanal + CoA + NAD(P)+
-
Substrates: -
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
oleoyl-[acyl carrier protein] + NAD(P)H + H+
oleic aldehyde + acyl carrier protein + NAD(P)+
oleoyl-[acyl carrier protein] + NADPH + H+
oleic aldehyde + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
stearoyl-[acyl carrier protein] + NADPH + H+
stearoylaldehyde + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
stearoyl-[acyl-carrier protein] + NAD(P)H + H+
stearylaldehyde + an [acyl-carrier protein] + NAD(P)+
additional information
?
-
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: kinetically preferred and likely the in vivo substrate
Products: -
?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: kinetically preferred and likely the in vivo substrate
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: acyl-CoA and acyl-ACP can serve as substrates
Products: hexadecanal is a reaction intermediate that is further converted into hexadecanol
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: substrate selectivity
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: acyl-ACP is kinetically preferred and is likely the in vivo substrate
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: substrate selectivity
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: acyl-ACP is kinetically preferred and is likely the in vivo substrate
Products: -
?
oleoyl-[acyl carrier protein] + NAD(P)H + H+
oleic aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: -
Products: -
?
oleoyl-[acyl carrier protein] + NAD(P)H + H+
oleic aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: -
Products: -
?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Substrates: -
Products: -
?
palmitoyl-CoA + NADPH + H+
hexadecanal + CoA + NADP+
Substrates: -
Products: -
?
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
-
Substrates: specific substrate
Products: -
?
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Substrates: -
Products: -
?
stearoyl-CoA + NADPH + H+
octadecanal + CoA + NADP+
Substrates: -
Products: -
?
stearoyl-[acyl-carrier protein] + NAD(P)H + H+
stearylaldehyde + an [acyl-carrier protein] + NAD(P)+
Substrates: -
Products: the enzyme specifically transfers the pro-R hydride of NADPH to the Cys294-thioester intermediate to afford its aldehyde product
?
stearoyl-[acyl-carrier protein] + NAD(P)H + H+
stearylaldehyde + an [acyl-carrier protein] + NAD(P)+
Substrates: -
Products: the enzyme specifically transfers the pro-R hydride of NADPH to the Cys294-thioester intermediate to afford its aldehyde product
?
additional information
?
-
-
Substrates: in Saccharomyces cerevisiae overexpressed truncated version of AtFAR6, which lacks the N-terminal extension, produces C16:0 primary fatty alcohol as well as C18:0 fatty alcohols much more efficiently than the full length protein
Products: -
?
additional information
?
-
-
Substrates: because of technical difficulties in preparing the native substrates for CpFAS1-R, which are very long chain fatty acyl-ACPs, long chain and very long chain fatty acyl-CoAs are used as substrates to assay CpFAS1-R activity
Products: -
?
additional information
?
-
-
Substrates: does not reduce acyl-CoA
Products: -
?
additional information
?
-
-
Substrates: does not reduce acyl-CoA
Products: -
?
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a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+
a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+
-
Substrates: -
Products: -
?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl-carrier protein + NAD(P)+
-
Substrates: -
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
oleoyl-[acyl carrier protein] + NADPH + H+
oleic aldehyde + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
stearoyl-[acyl carrier protein] + NADPH + H+
stearoylaldehyde + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: kinetically preferred and likely the in vivo substrate
Products: -
?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
-
Substrates: kinetically preferred and likely the in vivo substrate
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: acyl-ACP is kinetically preferred and is likely the in vivo substrate
Products: -
?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
-
Substrates: acyl-ACP is kinetically preferred and is likely the in vivo substrate
Products: -
?
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
-
Substrates: specific substrate
Products: -
?
palmitoyl-[acyl carrier protein] + NADPH + H+
hexadecanal + acyl carrier protein + NADP+
-
Substrates: -
Products: -
?
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C294S
the mutant avoids spontaneous formation of the acyl-enzyme intermediate
K80A
the mutant does not bind to aldehyde-deformylating oxygenase
R73A
the mutant does not bind to aldehyde-deformylating oxygenase
R79A
the mutant does not bind to aldehyde-deformylating oxygenase
Y247A
the inactive mutant does not bind to aldehyde-deformylating oxygenase
Y247F
the mutant shows strongly increased activity compared to the wild type enzyme
C294S
-
the mutant avoids spontaneous formation of the acyl-enzyme intermediate
-
K80A
-
the mutant does not bind to aldehyde-deformylating oxygenase
-
R73A
-
the mutant does not bind to aldehyde-deformylating oxygenase
-
R79A
-
the mutant does not bind to aldehyde-deformylating oxygenase
-
Y247F
-
the mutant shows strongly increased activity compared to the wild type enzyme
-
additional information
-
replacement of the PC7942_orf1593 and 1594 orthologues in Synechocystis sp. PCC6803, where the orthologous genes apparently form only a bicistronic operon, with a kanamycin-resistance cassette. This replacement abolishes the presence of alkanes in the extracts of photoautoptrophically grown cells. PCC7942_orf 1593 and orf1594 coexpression in an Escherichia coli strain devoid of acyl-CoAs leads to very similar levels of hydrocarbon production, comparable to those in an Escherichia coli wild-type strain
additional information
-
replacement of the PC7942_orf1593 and 1594 orthologues in Synechocystis sp. PCC6803, where the orthologous genes apparently form only a bicistronic operon, with a kanamycin-resistance cassette. This replacement abolishes the presence of alkanes in the extracts of photoautoptrophically grown cells. PCC7942_orf 1593 and orf1594 coexpression in an Escherichia coli strain devoid of acyl-CoAs leads to very similar levels of hydrocarbon production, comparable to those in an Escherichia coli wild-type strain
-
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AtFAR6 full length version and a truncated version, mAtFAR6, which lacks the chloroplast transit peptide sequence expressed in Escherichia coli, both enzymes fused at the C-terminus to a His Tag containing maltose binding protein
-
AtFAR6 full length version and a truncated version, mAtFAR6, which lacks the chloroplast transit peptide sequence subcloned into the pYES-DEST52 plasmid downstream of the GAL1 promoter and transformed into Saccharomyces cerevisiae W303-1A strain
-
expession in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Rhodococcus opacus strain ROP3
-
expressed in Synechocystis sp. PCC 6803
-
expression of strain PCC7942 orf1593 and orf1594, the latter encoding an aldehde decarbonylase, both separately and together in Escherichia coli. Extracts of recombinant PCC7942_orf1594-expressing cells contain substantial quantities of evenchain fatty aldehydes and fatty alcohols, whereas coexpression of both PCC7942_orf1593 and orf1594 results in the production of odd chain alkanes and alkenes, as well as even-chain fatty aldehydes and fatty alcohols. Orf1593 and orf1594 appear to be part of a larger operon that contains a gene encoding a subunit of the acetyl-CoA carboxylase, accA, which is essential for growth
-
in a Rosetta bacterial strain serving as an expression host for the maltose-binding protein-CpFAS1-R fusion protein
-
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Schirmer, A.; Rude, M.A.; Li, X.; Popova, E.; del Cardayre, S.B.
Microbial biosynthesis of alkanes
Science
329
559-562
2010
Synechococcus elongatus, Synechococcus elongatus PCC 7942, Synechococcus sp., Synechococcus sp. PCC 7942
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
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
Warui, D.M.; Pandelia, M.E.; Rajakovich, L.J.; Krebs, C.; Bollinger, J.M.; Booker, S.J.
Efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase
Biochemistry
54
1006-1015
2015
Nostoc punctiforme (B2J1M0), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 (B2J1M0)
brenda
Kaczmarzyk, D.; Cengic, I.; Yao, L.; Hudson, E.P.
Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX
Metab. Eng.
45
59-66
2018
Oryza sativa, Synechocystis sp. PCC 6803
brenda
Kim, H.M.; Chae, T.U.; Choi, S.Y.; Kim, W.J.; Lee, S.Y.
Engineering of an oleaginous bacterium for the production of fatty acids and fuels
Nat. Chem. Biol.
15
721-729
2019
Synechococcus elongatus
brenda
Gao, Y.; Zhang, H.; Fan, M.; Jia, C.; Shi, L.; Pan, X.; Cao, P.; Zhao, X.; Chang, W.; Li, M.
Structural insights into catalytic mechanism and product delivery of cyanobacterial acyl-acyl carrier protein reductase
Nat. Commun.
11
1525
2020
Synechococcus elongatus (Q54765), Synechococcus elongatus PCC 7942 (Q54765)
brenda
Sharma, A.; Shakeel, T.; Gupta, M.; Rajacharya, G.; Yazdani, S.
Biophysical and structural studies reveal marginal stability of a crucial hydrocarbon biosynthetic enzyme acyl ACP reductase
Sci. Rep.
11
12045
2021
Synechococcus elongatus (Q54765), Synechococcus elongatus PCC 7942 (Q54765)
brenda