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Information on EC 4.1.99.5 - aldehyde oxygenase (deformylating) and Organism(s) Nostoc punctiforme and UniProt Accession B2J1M1
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4.1.99.5 aldehyde oxygenase (deformylating)IUBMB Comments
Contains a diiron center. Involved in the biosynthesis of alkanes. The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 and C17 alkanes [2,3]. The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents . The substrate for this enzyme is formed by EC 1.2.1.80, acyl-[acyl-carrier protein] reductase.
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Word Map
- 4.1.99.5
-
biofuels
-
decarbonylation
-
acyl-acyl
- punctiforme
- elongatus
- octadecanal
-
di-iron
-
drop-in
-
cados
- heptadecane
-
ferritin-like
- prochlorococcus
-
diferric
-
photodecarboxylase
-
petroleum-derived
- biofuel production
The taxonomic range for the selected organisms is: Nostoc punctiforme
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
decarbonylase, aldehyde-deformylating oxygenase, aldehyde deformylating oxygenase, aldehyde decarbonylase, cyanobacterial aldehyde deformylating oxygenase, cado-1593, cyanobacterial aldehyde decarbonylase, cyanobacterial aldehyde-deformylating oxygenase, liado, osado, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde decarbonylase
decarbonylase
-
-
-
-
additional information
-
the cyanobacterial aldehyde decarbonylases belong to the family of alpha-helical ferritin-like proteins that harbor carboxylate-bridged dimetal (most often diiron) cofactors
aldehyde decarbonylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
the catalytic mechanism involves attack on the carbonyl of the bound substrate by the reduced O2 moiety to form a Fe2 III/III peroxyhemiacetal complex, which undergoes reductive O-O-bond cleavage, leading to C1-C2 radical fragmentation and formation of the alk(a/e)ne and formate products, detailed overview
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism via radical and Fe2 III/III?PHA intermediate, reaction overview
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
possible reaction mechanism, overview. Formate is the coproduct of alkane production by the Np AD, (ii) the aldehyde hydrogen of the substrate is retained in the formate, and (iii) the hydrogen added to C2 derives (at least in part) from solvent
-
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
mechanistic proposal for the oxygen-independent formation of alkanes by the enzyme. In this mechanism the external reducing system functions catalytically to generate a reactive ketyl radical anion and facilitate carbon-carbon bond cleavage
-
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
proposed mechanism of cADO involving homolytic cleavage of the C1-C2 bond of aldehyde by di-iron peroxo species, and proposed mechanism for deformylation involving heterolytic cleavage of the C1-C2 bond
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
a long-chain aldehyde alkane-lyase
Contains a diiron center. Involved in the biosynthesis of alkanes. The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 and C17 alkanes [2,3]. The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents [1]. The substrate for this enzyme is formed by EC 1.2.1.80, acyl-[acyl-carrier protein] reductase.
CAS REGISTRY NUMBER
COMMENTARY
94185-90-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
n-butanal + O2 + 2 NADPH + 2 H+
n-propane + formate + H2O + 2 NADP+
-
-
-
?
n-decanal + O2 + 2 NADPH + 2 H+
n-nonane + formate + H2O + 2 NADP+
-
-
-
?
n-hexadecanal + O2 + 2 NADPH + 2 H+
pentadecane + formate + H2O + 2 NADP+
-
-
-
?
n-hexanal + O2 + 2 NADPH + 2 H+
n-pentane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecenal + O2 + 2 NADPH + 2 H+
1-heptadecene + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
octanal + O2 + 2 NADH + 2 H+
heptane + formate + H2O + 2 NAD+
with reducing system NADH/phenazine methosulfate, reaction under anaerobic conditions to protect the cofactor, but the enzyme shows no differences between aerobic and anaerobic condition, meaning that the substrate does not bind tightly to the Fe2 III/III form of the enzyme or that the aldehyde binds in a manner that does not detectably alter its Moessbauer properties
GC-MS poduct analysis
-
?
2-(2-tetradecylcyclopropyl)acetaldehyde + 2 NADH + O2 + 2 H+
1-methyl-2-tetradecylcyclopropane + formate + H2O + 2 NAD+
-
formation of 1-octadecene at low level appears to be described by first-order kinetics, 1-octadecene might be involved in enzyme inhibition
GC-MS poduct analysis
-
?
dodecanal + O2 + 2 NADH + 2 H+
undecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
-
-
?
fatty aldehyde + O2 + NADPH
alkane + formate + H2O + NADP+
-
reaction requires dioxygen and results in incorporation of 18O from 18O2 into formate, activity depends on the presence of a reducing system (NADPH, ferredoxin and ferredoxin reductase)
-
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
-
-
-
-
?
pentadecanal + O2 + 2 NADH + 2 H+
tetradecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
trans-3-nonyloxirane-2-carbaldehyde + 2 NADH + 2 H+
2-nonyloxirane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
-
-
?
trans-3-pentadecanyloxirane-2-carbaldehyde + 2 NADH + O2 + 2 H+
2-pentadecanyloxirane + formate + 2 NAD+ + H2O
-
with reducing system NADH/phenazine methosulfate
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
ADO activity is dependent upon a continuous supply of electrons, both for reduction of the Fe2 III/III form of the cofactor back to the O2-reactive Fe2 II/II state and during conversion of the Fe2 III/III-PHA intermediate state to the product complex
-
-
?
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
-
activity depends on the presence of a reducing system (NADPH, ferredoxin and ferredoxin reductase)
-
-
?
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
-
only observed in the presence of ferredoxin, ferredoxin reductase and NADPH
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
GC-MS poduct analysis
-
?
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
-
?
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
the in vitro activity of the enzyme depends on the presence of a reducing system, i.e. NADPH, ferredoxin, and ferredoxin reductase
-
-
?
additional information
?
-
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
-
-
?
additional information
?
-
-
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
-
-
?
additional information
?
-
aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism. Both the diferric form of Nostoc punctiforme ADO and its (putative) diferric-peroxyhemiacetal intermediate are reduced much more rapidly by Synechocystis sp. PCC6803 PetF than by the previously employed chemical reductant, 1-methoxy-5-methylphenazinium methyl sulfate. The yield of formate and alkane per reduced PetF approaches its theoretical upper limit when reduction of the intermediate is carried out in the presence of FNR. Reduction of the intermediate by either system leads to accumulation of a substrate-derived peroxyl radical as a result of off-pathway trapping of the C2-alkyl radical intermediate by excess O2, which consequently diminishes the yield of the hydrocarbon product. A sulfinyl radical located on residue Cys71 also accumulates with short-chain aldehydes
-
-
?
additional information
?
-
-
aldehyde-deformylating oxygenase (ADO) catalyzes conversion of a fatty aldehyde to the corresponding alk(a/e)ne and formate, consuming four electrons and one molecule of O2 per turnover and incorporating one atom from O2 into the formate coproduct. A cyanobacterial [2Fe-2S] ferredoxin (PetF), reduced by ferredoxin-NADP+ reductase (FNR) using NADPH, is implicated. Rapid reduction of the diferric-peroxyhemiacetal intermediate in ADO by a cyanobacterial ferredoxin. The enzyme follows a free-radical mechanism. Both the diferric form of Nostoc punctiforme ADO and its (putative) diferric-peroxyhemiacetal intermediate are reduced much more rapidly by Synechocystis sp. PCC6803 PetF than by the previously employed chemical reductant, 1-methoxy-5-methylphenazinium methyl sulfate. The yield of formate and alkane per reduced PetF approaches its theoretical upper limit when reduction of the intermediate is carried out in the presence of FNR. Reduction of the intermediate by either system leads to accumulation of a substrate-derived peroxyl radical as a result of off-pathway trapping of the C2-alkyl radical intermediate by excess O2, which consequently diminishes the yield of the hydrocarbon product. A sulfinyl radical located on residue Cys71 also accumulates with short-chain aldehydes
-
-
?
additional information
?
-
GC-MS analysis of the volatile alkane products
-
-
?
additional information
?
-
GC-MS measurements and identification of products
-
-
?
additional information
?
-
-
the aldehyde hydrogen is retained in the HCO2- and the hydrogen in the nascent methyl group of the alkane originates, at least in part, from solvent. The reaction appears to be formally hydrolytic, but the improbability of a hydrolytic mechanism having the primary carbanion as the leaving group, the structural similarity of the aldehyde decarbonylases to other O2-activating non-heme di-iron proteins, and the dependence of in vitro aldehyde decarbonylase activity on the presence of a reducing system implicate some type of redox mechanism. Two possible resolutions to this conundrum, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate. The reaction requires an external reducing system but does not require oxygen. The enzyme catalyzes aldehyde decarbonylation at a much faster rate under anaerobic conditions, and the oxygen in formate derives from water. Eventhough an oxygen-dependent mechanism may operate in cAD, the oxygen-independent decarbonylation of aldehydes is a general feature of these enzymes
-
-
?
additional information
?
-
-
the enzyme is more active with either long-chain (C18-C14) or short-chain (C9-C5) aldehydes whereas medium chain aldehydes, including dodecanal, are turned over considerably more slowly
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
-
-
-
-
?
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
-
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
?
-
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
-
-
?
additional information
?
-
-
cyanobacterial aldehyde-deformylating oxygenases catalyze conversion of saturated or monounsaturated Cn fatty aldehydes to formate and the corresponding Cn-1 alkanes or alkenes, respectively
-
-
?
additional information
?
-
-
the aldehyde hydrogen is retained in the HCO2- and the hydrogen in the nascent methyl group of the alkane originates, at least in part, from solvent. The reaction appears to be formally hydrolytic, but the improbability of a hydrolytic mechanism having the primary carbanion as the leaving group, the structural similarity of the aldehyde decarbonylases to other O2-activating non-heme di-iron proteins, and the dependence of in vitro aldehyde decarbonylase activity on the presence of a reducing system implicate some type of redox mechanism. Two possible resolutions to this conundrum, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
identification of Synechocystis sp. PC 6803 ssl0020 ferredoxin, PetF, UniProt ID P27320, as an efficient ADO reductant, overview
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
Fe2+
di-iron enzyme, Moessbauer spectrum of the cofactor during the reaction steps, coordinations of the different cofactor states, e.g. the peroxo-Fe2 III/III intermediate, Fe2 III/III peroxyhemiacetal complex, or a micro-oxo-Fe2 III/III cluster, detailed overview
Fe2+
di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-tetradecylcyclopropyl)acetaldehyde
-
a cyclopropyl analogue of octadecanal in which the cyclopropyl group is positioned beta to the carbonyl group. The compound is partitioned between turnover and irreversible inhibition of the enzyme, mechanism of inactivation, overview. Formation of 1-octadecene at low level appears to be described by first-order kinetics might be involved in enzyme inhibition
additional information
-
trans-3-nonyloxirane-2-carbaldehyde and trans-3-pentadecanyloxirane-2-carbaldehyde are no inhibitors of the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the Nostoc punctiforme enzyme is triggered by short-chain (C6-C10) n-aldehyde substrates4 for addition of O2 to its Fe2 II/II cofactor
-
additional information
-
the Nostoc punctiforme enzyme is triggered by short-chain (C6-C10) n-aldehyde substrates4 for addition of O2 to its Fe2 II/II cofactor
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
complex kinetics of formation of the reaction intermediate, overview
-
additional information
additional information
-
complex kinetics of formation of the reaction intermediate, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
cyanobacterial aldehyde-deformylating oxygenases belong to the ferritin-like diiron-carboxylate superfamily of dioxygen-activating proteins
malfunction
C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview
metabolism
efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase in a two-step pathway consisting of an acyl-acyl carrier protein (ACP) reductase (AAR) and an aldehyde-deformylating oxygenase (ADO) allowing various cyanobacteria to convert long-chain fatty acids into hydrocarbons. When the aldehyde substrate is supplied to ADO by AAR, efficient in vitro turnover is observed in the absence of solubilizing agents, even with insoluble substrates like octadec(a/e)nal, overview. AAR and ADO form a tight isolable complex with a Kd of 0.003 mM. The interaction between AAR and ADO facilitates either direct transfer of the aldehyde product of AAR to ADO or formation of the aldehyde product in a microenvironment allowing for its efficient uptake by ADO
physiological function
metabolism
-
in cyanobacteria, aldehyde deformylating oxygenase catalyzes the decarbonylation of fatty aldehydes to the corresponding alkanes or alkenes, last step in the biosynthesis of long-chain aliphatic hydrocarbons, which are derived from fatty acids
physiological function
additional information
physiological function
aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria
physiological function
aldehyde-deformylating oxygenase (ADO) is a ferritin-like nonheme-diiron enzyme that catalyzes the last step in a pathway through which fatty acids are converted into hydrocarbons in cyanobacteria
physiological function
aldehyde-deformylating oxygenase (ADO) is an important enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. ADO transforms the fatty aldehyde to a Cn-1 hydrocarbon and C1-derived formate
physiological function
-
saturated fatty acids are converted to alkanes (and unsaturated fatty acids to alkenes) in cyanobacteria entailing scission of the C1-C2 bond of a fatty aldehyde intermediate by the enzyme aldehyde decarbonylase. The in vitro activity of the enzyme depends on the presence of a reducing system, i.e. NADPH, ferredoxin, and ferredoxin reductase
additional information
Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme
additional information
-
the very low activity of the enzyme appears to result from inhibition by the ferredoxin reducing system used in the assay and the low solubility of the substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C107A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C107A/C117A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C117A
site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme
C71A
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
C71A/C107A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71A/C107A/C117A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71A/C117A
site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant
C71S
site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme
additional information
installation of a recombinant hydrocarbon production system in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr for production of n-alkanes by a combinant ion of four enzymes, i.e. aldehyde deformylating oxygenase (from Nostoc punctiforme ), ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), method optimization and evaluation, overview. GC-MS analysis of the volatile alkanes produced. Comparison of ADO orthologues from different origins in hydrocarbon biosynthesis in vivo
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) in an anaerobic chamber, further by metal affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Npun_R1711, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)DELTAyqhDDELTAahr, simultaneous coexpression with four enzymes required in the alkane pathway: aldehyde deformylating oxygenase, ferredoxin (from Synechocystis), phosphopantetheinyl transferase (from Bacillus subtilis) and carboxylic acid reductase (from Mycobacterium marinum), expression analysis
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schirmer, A.; Rude, M.A.; Li, X.; Popova, E.; del Cardayre, S.B.
Microbial biosynthesis of alkanes
Science
329
559-562
2010
Nostoc punctiforme
Warui, D.M.; Li, N.; N?rgaard, H.; Krebs, C.; Bollinger, J.M.; Booker, S.J.
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase
J. Am. Chem. Soc.
133
3316-3319
2011
Nostoc punctiforme
Li, N.; Nrgaard, H.; Warui, D.M.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase
J. Am. Chem. Soc.
133
6158-6161
2011
Nostoc punctiforme
Das, D.; Ellington, B.; Paul, B.; Marsh, E.N.
Mechanistic insights from reaction of alpha-oxiranyl-aldehydes with cyanobacterial aldehyde deformylating oxygenase
ACS Chem. Biol.
9
570-577
2014
Nostoc punctiforme
Eser, B.E.; Das, D.; Han, J.; Jones, P.R.; Marsh, E.N.
Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor
Biochemistry
50
10743-10750
2011
Nostoc punctiforme, Prochlorococcus marinus, Prochlorococcus marinus MIT9313, Synechococcus sp., Synechocystis sp.
Pandelia, M.E.; Li, N.; Noergaard, H.; Warui, D.M.; Rajakovich, L.J.; Chang, W.C.; Booker, S.J.; Krebs, C.; Bollinger, J.M.
Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate
J. Am. Chem. Soc.
135
15801-15812
2013
Nostoc punctiforme (B2J1M1), Nostoc punctiforme
Paul, B.; Das, D.; Ellington, B.; Marsh, E.N.
Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde
J. Am. Chem. Soc.
135
5234-5237
2013
Nostoc punctiforme
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 (B2J1M1), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1)
Rajakovich, L.J.; N?rgaard, H.; Warui, D.M.; Chang, W.C.; Li, N.; Booker, S.J.; Krebs, C.; Bollinger, J.M.; Pandelia, M.E.
Rapid reduction of the diferric-peroxyhemiacetal intermediate in aldehyde-deformylating oxygenase by a cyanobacterial ferredoxin evidence for a free-radical mechanism
J. Am. Chem. Soc.
137
11695-11709
2015
Nostoc punctiforme (B2J1M1), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1)
Patrikainen, P.; Carbonell, V.; Thiel, K.; Aro, E.M.; Kallio, P.
Comparison of orthologous cyanobacterial aldehyde deformylating oxygenases in the production of volatile C3-C7 alkanes in engineered E. coli
Metab. Eng. Commun.
5
9-18
2017
Nostoc punctiforme (B2J1M1), Nostoc punctiforme ATCC 29133 / PCC 73102 (B2J1M1), Prochlorococcus marinus (Q7V6D4), Prochlorococcus marinus MIT 9313 (Q7V6D4), Synechococcus sp. RS9917 (A3Z5H6), Synechocystis sp. PCC 6803 (Q55688)
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