BRENDA - Enzyme Database
show all sequences of 4.1.99.5

Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor

Eser, B.E.; Das, D.; Han, J.; Jones, P.R.; Marsh, E.N.; Biochemistry 50, 10743-10750 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of N-terminally His-tagged enzyme in Escherichia coli
Nostoc punctiforme
expression of N-terminally His-tagged enzyme in Escherichia coli
Prochlorococcus marinus
expression of N-terminally His-tagged enzyme in Escherichia coli
Synechococcus sp.
expression of N-terminally His-tagged enzyme in Escherichia coli
Synechocystis sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
ethyl acetate
-
Nostoc punctiforme
ethyl acetate
-
Prochlorococcus marinus
ethyl acetate
-
Synechococcus sp.
ethyl acetate
-
Synechocystis sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Nostoc punctiforme
-
-
-
Prochlorococcus marinus
-
-
-
Prochlorococcus marinus MIT9313
-
-
-
Synechococcus sp.
-
-
-
Synechocystis sp.
-
-
-
Reaction
Reaction
Commentary
Organism
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
Nostoc punctiforme
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
Prochlorococcus marinus
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
Synechococcus sp.
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
Synechocystis sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechococcus sp.
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechocystis sp.
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Nostoc punctiforme
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus MIT9313
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
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
726957
Synechococcus sp.
?
-
-
-
-
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
726957
Synechocystis sp.
?
-
-
-
-
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
726957
Prochlorococcus marinus
?
-
-
-
-
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
726957
Nostoc punctiforme
?
-
-
-
-
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
726957
Prochlorococcus marinus MIT9313
?
-
-
-
-
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechococcus sp.
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechocystis sp.
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Nostoc punctiforme
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus MIT9313
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Nostoc punctiforme
37
-
assay at
Prochlorococcus marinus
37
-
assay at
Synechococcus sp.
37
-
assay at
Synechocystis sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Nostoc punctiforme
7.2
-
assay at
Prochlorococcus marinus
7.2
-
assay at
Synechococcus sp.
7.2
-
assay at
Synechocystis sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Synechococcus sp.
NADH
-
Synechocystis sp.
NADH
-
Prochlorococcus marinus
NADH
-
Nostoc punctiforme
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of N-terminally His-tagged enzyme in Escherichia coli
Nostoc punctiforme
expression of N-terminally His-tagged enzyme in Escherichia coli
Prochlorococcus marinus
expression of N-terminally His-tagged enzyme in Escherichia coli
Synechococcus sp.
expression of N-terminally His-tagged enzyme in Escherichia coli
Synechocystis sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Synechococcus sp.
NADH
-
Synechocystis sp.
NADH
-
Prochlorococcus marinus
NADH
-
Nostoc punctiforme
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ethyl acetate
-
Nostoc punctiforme
ethyl acetate
-
Prochlorococcus marinus
ethyl acetate
-
Synechococcus sp.
ethyl acetate
-
Synechocystis sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechococcus sp.
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechocystis sp.
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Nostoc punctiforme
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
heptanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus MIT9313
hexane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
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
726957
Synechococcus sp.
?
-
-
-
-
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
726957
Synechocystis sp.
?
-
-
-
-
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
726957
Prochlorococcus marinus
?
-
-
-
-
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
726957
Nostoc punctiforme
?
-
-
-
-
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
726957
Prochlorococcus marinus MIT9313
?
-
-
-
-
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechococcus sp.
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Synechocystis sp.
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Nostoc punctiforme
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
octadecanal + O2 + 2 NADH + 2 H+
with reducing system NADH/phenazine methosulfate or reducing system with NADPH, ferredoxin, and ferredoxin reductase
726957
Prochlorococcus marinus MIT9313
heptadecane + formate + H2O + 2 NAD+
GC-MS poduct analysis
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Nostoc punctiforme
37
-
assay at
Prochlorococcus marinus
37
-
assay at
Synechococcus sp.
37
-
assay at
Synechocystis sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Nostoc punctiforme
7.2
-
assay at
Prochlorococcus marinus
7.2
-
assay at
Synechococcus sp.
7.2
-
assay at
Synechocystis sp.
General Information
General Information
Commentary
Organism
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
Nostoc punctiforme
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
Prochlorococcus marinus
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
Synechococcus sp.
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
Synechocystis sp.
General Information (protein specific)
General Information
Commentary
Organism
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
Nostoc punctiforme
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
Prochlorococcus marinus
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
Synechococcus sp.
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
Synechocystis sp.
Other publictions for EC 4.1.99.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747409
Wang
Identification of residues im ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2, Synechocystis sp. PCC 6803
BMC Biotechnol.
17
31-39
2017
-
-
-
-
21
-
-
8
-
2
-
3
-
9
-
-
-
-
-
-
-
-
11
1
-
-
-
28
-
-
-
1
-
-
-
-
-
-
1
-
21
-
-
-
-
8
-
2
-
3
-
-
-
-
-
-
-
-
11
1
-
-
-
28
-
-
-
-
-
2
2
-
9
9
748564
Patrikainen
Comparison of orthologous cya ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102, Prochlorococcus marinus, Prochlorococcus marinus MIT 9313, Synechococcus sp. RS9917, Synechocystis sp. PCC 6803
Metab. Eng. Commun.
5
9-18
2017
-
-
4
-
5
-
-
-
-
-
-
6
-
13
-
-
-
-
-
-
-
-
30
-
-
-
-
-
-
-
-
4
-
-
-
-
-
4
4
-
5
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
30
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746976
Park
Crystal structures of aldehyd ...
Limnothrix redekei, Limnothrix redekei KNUA012, Oscillatoria sp. KNUA011
Biochem. Biophys. Res. Commun.
477
395-400
2016
-
2
2
2
-
-
-
-
-
-
-
3
-
5
-
-
-
-
-
-
-
-
6
2
2
-
-
-
2
-
-
2
-
-
-
-
2
2
2
2
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
6
2
2
-
-
-
2
-
-
-
-
4
4
-
-
-
747351
Bao
Structure-oriented substrate ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Biotechnol. Biofuels
9
185
2016
-
-
1
-
13
-
-
7
-
-
-
2
-
6
-
-
1
-
-
-
-
-
14
-
1
-
-
8
1
-
-
1
-
-
-
-
-
1
1
-
13
-
-
-
-
7
-
-
-
2
-
-
-
1
-
-
-
-
14
-
1
-
-
8
1
-
-
-
-
2
2
-
8
8
747353
Zhang
Microbial synthesis of propan ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
Biotechnol. Biofuels
9
80
2016
-
-
1
-
3
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
747081
Warui
Efficient delivery of long-ch ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
Biochemistry
54
1006-1015
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
748027
Rajakovich
Rapid reduction of the diferr ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
J. Am. Chem. Soc.
137
11695-11709
2015
-
-
-
-
-
-
-
-
-
1
-
2
-
8
-
-
-
1
-
-
-
-
10
-
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
10
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
748032
Shokri
Conversion of aldehyde to alk ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
J. Am. Chem. Soc.
137
7686-7691
2015
-
1
-
-
-
-
-
-
-
1
-
2
-
6
-
-
-
1
-
-
-
-
8
1
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
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8
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Role of cysteine residues in ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
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Jia
Structural insights into the ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
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2015
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Mechanistic insights from reac ...
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746597
Buer
Insights into substrate and m ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
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2014
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Waugh
Solvent isotope effects on al ...
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726548
Aukema
Cyanobacterial aldehyde deform ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
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2013
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727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus
Biotechnol. Biofuels
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727312
Khara
Production of propane and othe ...
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2013
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727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
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727693
Paul
Probing the mechanism of cyano ...
Nostoc punctiforme
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2013
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727001
Li
Evidence for only oxygenative ...
Prochlorococcus marinus
Biochemistry
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2012
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715293
Warui
Detection of formate, rather t ...
Nostoc punctiforme
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2011
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715300
Li
Conversion of fatty aldehydes ...
Nostoc punctiforme
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2011
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726957
Eser
Oxygen-independent alkane form ...
Nostoc punctiforme, Prochlorococcus marinus, Prochlorococcus marinus MIT9313, Synechococcus sp., Synechocystis sp.
Biochemistry
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10743-10750
2011
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713511
Schirmer
Microbial biosynthesis of alka ...
Nostoc punctiforme
Science
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2010
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Schneider-Belhaddad
Solubilization, partial purifi ...
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Arch. Biochem. Biophys.
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2000
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Kobayashi
Cobalt proteins ...
Botryococcus braunii
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648394
Dennis
A cobalt-porphyrin enzyme conv ...
Botryococcus braunii, Botryococcus braunii Austin
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5306-5310
1992
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Dennis
Alkane biosynthesis by decarbo ...
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Cheesbrough
Microsomal preparation from an ...
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648391
Cheesbrough
Alkane biosynthesis by decarbo ...
Pisum sativum
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