Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lin, F.; Das, D.; Lin, X.N.; Marsh, E.N.
    Aldehyde-forming fatty acyl-CoA reductase from cyanobacteria expression, purification and characterization of the recombinant enzyme (2013), FEBS J., 280, 4773-4781 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.1.B25 bovine serum albumin activates 3fold at 1 mg/ml Synechococcus elongatus
1.2.1.B25 CHAPS activates about by 75% at 0.2%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 Digitonin activates about at 0.1%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 octyl glucoside activates slightly about at 0.2%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 tris(hydroxypropyl)phosphine activates 2fold at 20 mM Synechococcus elongatus

Application

EC Number Application Comment Organism
1.2.1.B25 biofuel production long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes. As such they are attractive as components in engineered metabolic pathways for drop in biofuels. The slow turnover number measured for Synechococcus elongatus ACR poses a challenge for its use in biofuel applications where highly efficient enzymes are needed Synechococcus elongatus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.B25 recombinant overexpression of His-tagged enzyme in Escherichia coli Synechococcus elongatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.B25 CHAPS activates about by 75% at 0.2%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 Digitonin activates about at 0.1%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 dithiothreitol inhibits the enzyme at 5 mM Synechococcus elongatus
1.2.1.B25 glutathione inhibits the enzyme at 5 mM Synechococcus elongatus
1.2.1.B25 iodoacetamide inactivation at 1 mM, stearoyl-CoA protects, probably due to competition between the two reagents for the active site cysteine Synechococcus elongatus
1.2.1.B25 additional information once acylated by stearoyl-CoA the enzyme is protected from inactivation by iodoacetamide and the cACR activity remains unchanged Synechococcus elongatus
1.2.1.B25 octyl glucoside activates slightly about at 0.2%, inhibitory at above 0.5% Synechococcus elongatus
1.2.1.B25 Triton inhibitory at above 0.5% Synechococcus elongatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.B25 additional information
-
 additional information steady-state kinetic analysis Synechococcus elongatus
1.2.1.B25 0.0319
-
 stearoyl-CoA pH 7.5, 37°C, recombinant enzyme Synechococcus elongatus
1.2.1.B25 0.0356
-
 NADPH pH 7.5, 37°C, recombinant enzyme Synechococcus elongatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.B25 cytosol
-
 Synechococcus elongatus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.B25 Ca2+ activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 5 mM Synechococcus elongatus
1.2.1.B25 K+ activates about 10fold Synechococcus elongatus
1.2.1.B25 Mg2+ best activating divalent cation Synechococcus elongatus
1.2.1.B25 Mn2+ activates, inhibitory as it causes precipitation of the acyl-CoA substrate at 2 mM Synechococcus elongatus
1.2.1.B25 additional information ACR requires divalent metal ions for activity. 2-mercaptoethanol and Na+ have no effect on activity Synechococcus elongatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.B25 stearoyl-CoA + NADPH Synechococcus elongatus
-
 octadecanal + CoA + NADP+
-
 ?
1.2.1.B25 stearoyl-CoA + NADPH Synechococcus elongatus PCC7942
-
 octadecanal + CoA + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.B25 Synechococcus elongatus
-
-
-
1.2.1.B25 Synechococcus elongatus PCC7942
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.B25 recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Synechococcus elongatus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.B25 hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH the enzyme operates by a Ping-Pong mechanism Synechococcus elongatus
a

Storage Stability

EC Number Storage Stability Organism
1.2.1.B25 -80°C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4°C, although it can be stored for prolonged periods at -80°C without loss of activity Synechococcus elongatus
1.2.1.B25 4°C, purified cACR is quite unstable and tends to precipitate after 3-4 days when stored at 4°C, although it can be stored for prolonged periods at -80°C without loss of activity Synechococcus elongatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.B25 dodecanoyl-CoA + NADPH low activity Synechococcus elongatus dodecanal + CoA + NADP+
-
 ?
1.2.1.B25 dodecanoyl-CoA + NADPH low activity Synechococcus elongatus PCC7942 dodecanal + CoA + NADP+
-
 ?
1.2.1.B25 eicosanoyl-CoA + NADPH
-
 Synechococcus elongatus eicosanal + CoA + NADP+
-
 ?
1.2.1.B25 hexadecanoyl-CoA + NADPH + H+ low activity Synechococcus elongatus hexadecanal + CoA + NADP+
-
 ?
1.2.1.B25 hexadecanoyl-CoA + NADPH + H+ low activity Synechococcus elongatus PCC7942 hexadecanal + CoA + NADP+
-
 ?
1.2.1.B25 additional information the enzyme cACR is specific for NADPH and specifically catalyzes the reduction of fatty acyl-CoA esters to the corresponding aldehydes, rather than alcohols. Stearoyl-CoA is the most effective substrate, being reduced more rapidly than either longer or shorter chain acyl-CoAs. The enzyme is acylated on incubation with stearoyl-CoA, suggesting that the reduction occurs through an enzyme-thioester intermediate, cf. EC 1.2.1.50, formation of an acyl thioester on an active site cysteinyl residue as an intermediate in the mechanism of reduction. No activity with octanoyl-CoA Synechococcus elongatus ?
-
 ?
1.2.1.B25 additional information the enzyme cACR is specific for NADPH and specifically catalyzes the reduction of fatty acyl-CoA esters to the corresponding aldehydes, rather than alcohols. Stearoyl-CoA is the most effective substrate, being reduced more rapidly than either longer or shorter chain acyl-CoAs. The enzyme is acylated on incubation with stearoyl-CoA, suggesting that the reduction occurs through an enzyme-thioester intermediate, cf. EC 1.2.1.50, formation of an acyl thioester on an active site cysteinyl residue as an intermediate in the mechanism of reduction. No activity with octanoyl-CoA Synechococcus elongatus PCC7942 ?
-
 ?
1.2.1.B25 oleoyl-CoA + NADPH low activity Synechococcus elongatus (9Z)-octadecenal + CoA + NADP+
-
 ?
1.2.1.B25 stearoyl-CoA + NADPH
-
 Synechococcus elongatus octadecanal + CoA + NADP+
-
 ?
1.2.1.B25 stearoyl-CoA + NADPH best substrate. When the enzyme is incubated with both stearoyl-CoA and NADPH, the acyl-enzyme accumulates to comprise about 50% of the enzyme. This observation suggests that the rates of acylation and reduction are approximately the same Synechococcus elongatus octadecanal + CoA + NADP+
-
 ?
1.2.1.B25 stearoyl-CoA + NADPH
-
 Synechococcus elongatus PCC7942 octadecanal + CoA + NADP+
-
 ?
1.2.1.B25 stearoyl-CoA + NADPH best substrate. When the enzyme is incubated with both stearoyl-CoA and NADPH, the acyl-enzyme accumulates to comprise about 50% of the enzyme. This observation suggests that the rates of acylation and reduction are approximately the same Synechococcus elongatus PCC7942 octadecanal + CoA + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.B25 ? x * 42626, mass spectrometry and sequence calculation Synechococcus elongatus

Synonyms

EC Number Synonyms Comment Organism
1.2.1.B25 Acr
-
 Synechococcus elongatus
1.2.1.B25 aldehyde-forming fatty acyl-CoA reductase
-
 Synechococcus elongatus
1.2.1.B25 cACR
-
 Synechococcus elongatus
1.2.1.B25 cyanobacterial acyl-CoA reductase
-
 Synechococcus elongatus
1.2.1.B25 long-chain ACR
-
 Synechococcus elongatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.B25 37
-
 assay at Synechococcus elongatus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.B25 0.006
-
 stearoyl-CoA pH 7.5, 37°C, recombinant enzyme Synechococcus elongatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.B25 8
-
-
 Synechococcus elongatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.B25 additional information no activity with NADH Synechococcus elongatus
1.2.1.B25 NADPH specific for Synechococcus elongatus

General Information

EC Number General Information Comment Organism
1.2.1.B25 physiological function long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes Synechococcus elongatus