Information on EC 4.1.99.5 - aldehyde oxygenase (deformylating)

Word Map on EC 4.1.99.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.1.99.5
-
RECOMMENDED NAME
GeneOntology No.
aldehyde oxygenase (deformylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alkane biosynthesis I
-
-
Biosynthesis of secondary metabolites
-
-
cuticular wax biosynthesis
-
-
Cutin, suberine and wax biosynthesis
-
-
heptadecane biosynthesis
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Austin belonging to the A race
-
-
Manually annotated by BRENDA team
eared grebe
-
-
Manually annotated by BRENDA team
gene PMT_1231
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
cyanobacterial aldehyde-deformylating oxygenases belong to the ferritin-like diiron-carboxylate superfamily of dioxygen-activating proteins
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-(2-tetradecylcyclopropyl)acetaldehyde + 2 NADH + 2 H+
1-methyl-2-tetradecylcyclopropane + formate + H2O + 2 NAD+
show the reaction diagram
-
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
-
?
butanal + O2 + 2 NADH + 2 H+
propane + formate + H2O + 2 NAD+
show the reaction diagram
decanal + O2 + 2 NADH + 2 H+
nonane + formate + H2O + 2 NAD+
show the reaction diagram
dodecanal + O2 + 2 NADH + 2 H+
undecane + formate + H2O + 2 NAD+
show the reaction diagram
-
with reducing system NADH/phenazine methosulfate
-
-
?
fatty aldehyde + O2 + NADPH
alkane + formate + H2O + NADP+
show the reaction diagram
-
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 NAD(P)H + 2 H+
hexane + formate + H2O + 2 NAD(P)+
show the reaction diagram
-
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
-
-
?
heptanal + O2 + 2 NADH + 2 H+
hexane + formate + H2O + 2 NAD+
show the reaction diagram
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
-
-
?
nonanal + O2 + 2 NADH + 2 H+
octane + formate + H2O + 2 NAD+
show the reaction diagram
octadecanal
heptadecane + CO
show the reaction diagram
octadecanal + NADPH + O2
heptadecane + formate + H2O + NADP+
show the reaction diagram
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
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
heptadecane + formate + H2O + 2 NAD+
show the reaction diagram
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
show the reaction diagram
octanal + O2 + 2 NADH + 2 H+
heptane + formate + H2O + 2 NAD+
show the reaction diagram
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
-
?
pentadecanal + O2 + 2 NADH + 2 H+
tetradecane + formate + H2O + 2 NAD+
show the reaction diagram
-
with reducing system NADH/phenazine methosulfate
GC-MS poduct analysis
-
?
pentanal + O2 + 2 NADH + 2 H+
butane + formate + H2O + 2 NAD+
show the reaction diagram
trans-3-nonyloxirane-2-carbaldehyde + 2 NADH + 2 H+
2-nonyloxirane + formate + H2O + 2 NAD+
show the reaction diagram
-
with reducing system NADH/phenazine methosulfate
-
-
?
trans-3-pentadecanyloxirane-2-carbaldehyde + 2 NADH + 2 H+
2-pentadecanyloxirane + formate + H2O + 2 NAD+
show the reaction diagram
-
with reducing system NADH/phenazine methosulfate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
octadecanal + O2 + 2 NADPH + 2 H+
heptadecane + formate + H2O + 2 NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
probably a copper enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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
8-hydroxyquinoline
coenzyme A
-
0.2 mM
dithioerythritol
-
5 mM, complete inhibition
ethyl acetate
metal ion chelators
-
NADPH
-
presence causes 50% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
0.005 mM, 2.8fold stimulation
ascorbate
phopshatidylserine
-
requirement, phosphatidylcholine is preferred, phopshatidylserine and phopshatidylethanolamine substitute less effectively
phosphatidylcholine
-
requirement, preferred lipid, phopshatidylserine and phopshatidylethanolamine substitute less effectively
phosphatidylethanolamine
-
requirement, phosphatidylcholine is preferred, phopshatidylserine and phopshatidylethanolamine substitute less effectively
Phospholipid
-
requirement, dose-dependent stimulation, phosphatidylcholine is preferred, phopshatidylserine and phopshatidylethanolamine substitute less effectively
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 hide
LITERATURE
IMAGE
0.244
n-Heptanal
pH 7.2, 22C, recombinant enzyme with Fd/FNR system
0.035 - 0.18
Octadecanal
additional information
additional information
complex kinetics of formation of the reaction intermediate, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073
n-Heptanal
Synechococcus elongatus
Q54764
pH 7.2, 22C, recombinant enzyme with Fd/FNR system
0.0018
Octadecanal
Nostoc punctiforme
-
pH 7.2, 37C
0.00027
trans-3-nonyloxirane-2-carbaldehyde
Nostoc punctiforme
-
pH 7.2, 37C
0.00048
trans-3-pentadecanyloxirane-2-carbaldehyde
Nostoc punctiforme
-
pH 7.2, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000235
-
at room temperature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
additional information
-
assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
apical meristem and its enclosing unopened leaflets from 28-36 days old plants
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cuticle region
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Prochlorococcus marinus (strain MIT 9313)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26400
x * 26400, recombinant N-terminally His-tagged enzyme, SDS-PAGE
55000
-
x * 55000 + x * 66000, 2 bands, may be (alpha)n(beta)n structure, SDS-PAGE
66000
-
x * 55000 + x * 66000, 2 bands, may be (alpha)n(beta)n structure, SDS-PAGE
67000
-
x * 67000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete inactivation by freezing
-
sensitive to trypsin treatment
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inhibited in the presence of O2
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
208fold, solubilized with octyl beta-glucoside
-
partial, 1306fold, solubilized with beta-octyl glucoside
-
recombinant enzyme from Escherichia coli
-
recombinant enzyme mutants V41Y and A134F to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) in an anaerobic chamber, further by metal affinity chromatography
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography and dialysis
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
affinity-tagged version expressed in Escherichia coli
-
cloning of gene Synpcc7942_159 from strain PCC7942, overexpression of N-terminally His-tagged protein in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
-
expression of N-terminally His-tagged enzyme in Escherichia coli
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Npun_R1711, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
His-tagged version expressed in Escherichia coli; recombinant overexpression in Escherichia coli
-
overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression in Escherichia coli
-
recombinant expression of mutants V41Y and A134F
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A134F
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO
V41Y
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested
V41Y/A134F
-
site-directed mutagenesis, the double mutant shows reduced activity with long-chain aldehyde substrates and increased activity with short-chain aldehyde substrates like the single mutants
A134F
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO
-
V41Y
-
site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested
-
V41Y/A134F
-
site-directed mutagenesis, the double mutant shows reduced activity with long-chain aldehyde substrates and increased activity with short-chain aldehyde substrates like the single mutants
-
additional information
Show AA Sequence (228 entries)
Please use the Sequence Search for a specific query.