Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
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
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
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
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
C-terminal CpFAS1-R enzyme belongs to a multifunctional Type I fatty acid synthase, CpFAS1, with at least 21 enzymatic domains, this megasynthase is predicted to function as a fatty acyl elongase
enzyme and aldehyde-deformylating oxygenase ADO form a tight isolable complex with a Kd of 3 microM. When the aldehyde substrate is supplied to ADO by acyl-acyl carrier protein reductase, efficient in vitro turnover is observed in the absence of solubilizing agents. Catalysis by acyl-acyl carrier protein reductase proceeds via formation of a covalent intermediate involving residue C294. The enzyme specifically transfers the pro-R hydride of NADPH to the Cys294-thioester intermediate to afford its aldehyde product
the enzyme is involved in an alkane biosynthesis pathway. It forms a complex with aldehyde-deformylating oxygenase that efficiently converts long chain fatty acyl-ACP/fatty acyl-CoA into hydrocarbon
enzyme and aldehyde-deformylating oxygenase ADO form a tight isolable complex with a Kd of 3 microM. When the aldehyde substrate is supplied to ADO by acyl-acyl carrier protein reductase, efficient in vitro turnover is observed in the absence of solubilizing agents. Catalysis by acyl-acyl carrier protein reductase proceeds via formation of a covalent intermediate involving residue C294. The enzyme specifically transfers the pro-R hydride of NADPH to the Cys294-thioester intermediate to afford its aldehyde product
the enzyme is involved in an alkane biosynthesis pathway. It forms a complex with aldehyde-deformylating oxygenase that efficiently converts long chain fatty acyl-ACP/fatty acyl-CoA into hydrocarbon
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligand-free enzyme and three complex structures in which the enzyme binds to aldehyde-deformylating oxygenase and various ligands (stearoyl-CoA, NADPH, thioester), hanging drop vapor diffusion method, using 0.1 M citric acid, pH6.0, and 1 M (NH4)2SO4 (ligand-free enzyme) or 0.1 M HEPES, pH 7.5, and 20% (w/v) PEG8000 (enzyme in complex with ligands)
sitting-drop vapor diffusion method at 18°C, structure of the ligand-free enzyme, and three acyl-acyl carrier protein reductase/aldehyde-deformylating oxygenase complex structures in which acyl-acyl carrier protein reductase bind various ligands
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
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
since the giant CpFAS1 and polyketide synthase CpPKS1 are structurally and functionally different from human Type I FAS, these parasite megasynthases may serve as novel drug targets, also because CpFAS1 and CpPKS1 utilize R domains to release final products
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
Efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase
Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX