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Information on EC 4.1.99.5 - aldehyde oxygenase (deformylating) and Organism(s) Synechococcus elongatus and UniProt Accession Q54764

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.99 Other carbon-carbon lyases
                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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Synechococcus elongatus
UNIPROT: Q54764
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The taxonomic range for the selected organisms is: Synechococcus elongatus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide
octadecanal
+
O2
+
2
NADPH
+
2
H+
=
heptadecane
+
formate
+
H2O
+
2
NADP+
+
+
2
+
2
=
+
+
+
2
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde decarbonylase
UniProt
aldehyde-deformylating oxygenase
-
aldehyde decarbonylase
-
-
-
-
decarbonylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C bond cleavage
-
-
-
-
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 hide
94185-90-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hexadecanal + O2 + 2 NAD(P)H + 2 H+
pentadecane + formate + H2O + 2 NAD(P)+
show the reaction diagram
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
-
-
?
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
show the reaction diagram
-
-
-
?
n-heptanal + O2 + 2 NAD(P)H + 2 H+
n-hexane + formate + H2O + 2 NAD(P)+
show the reaction diagram
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
-
-
?
octadecanal + O2 + 2 NAD(P)H + 2 H+
heptadecane + formate + H2O + 2 NAD(P)+
show the reaction diagram
endogenous reducing system ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase
-
-
?
additional information
?
-
the endogenous electron transfer system works more effectively than the heterologous and chemical ones, e.g. phenazine methosulfate or 1-methyoxy-5-methylphenazinium methylsulfate and NADH, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
long-chain aldehyde + O2 + 2 NADPH + 2 H+
alkane + formate + H2O + 2 NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
physiological cofactor
additional information
ferredoxin-mediated the cytochrome c reduction with ferredoxin-NADP+ reductase: ADO is selective against ferredoxin and the interaction between ferredoxin and ferredoxin-NADP+ reductase is very important for efficient electron transfer and ADO activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.244
n-Heptanal
pH 7.2, 22°C, recombinant enzyme with Fd/FNR system
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073
n-Heptanal
pH 7.2, 22°C, recombinant enzyme with Fd/FNR system
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26400
x * 26400, recombinant N-terminally His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 26400, recombinant N-terminally His-tagged enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, removal of the tag by thrombin, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of gene Synpcc7942_159 from strain PCC7942, overexpression of N-terminally His-tagged protein in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, J.; Lu, X.; Li, J.J.
Conversion of fatty aldehydes into alk (a/e)nes by in vitro reconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system
Biotechnol. Biofuels
6
86
2013
Synechococcus elongatus (Q54764), Synechococcus elongatus PCC 7942 (Q54764)
Manually annotated by BRENDA team