BRENDA - Enzyme Database
show all sequences of 4.1.99.5

Conversion of aldehyde to alkane by a peroxoiron(III) complex a functional model for the cyanobacterial aldehyde-deformylating oxygenase

Shokri, A.; Que, L.; J. Am. Chem. Soc. 137, 7686-7691 (2015)

Data extracted from this reference:

Application
Application
Commentary
Organism
biofuel production
the conversion of long-chain fatty aldehydes to corresponding alkanes, that is catalyzed by cyanobacterial aldehyde-deformylating oxygenase (cADO), is probably useful for production of biofuel
Prochlorococcus marinus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
nonheme di-iron center
Prochlorococcus marinus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus MIT 9313
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Prochlorococcus marinus
Q7V6D4
-
-
Prochlorococcus marinus MIT 9313
Q7V6D4
-
-
Reaction
Reaction
Commentary
Organism
Reaction ID
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
reaction mechanism, overview
Prochlorococcus marinus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
748032
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
748032
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
748032
Prochlorococcus marinus
?
-
-
-
-
additional information
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
748032
Prochlorococcus marinus MIT 9313
?
-
-
-
-
n-undecanal + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus
n-decane + formate + H2O + 2 NADP+
-
-
-
?
n-undecanal + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus MIT 9313
n-decane + formate + H2O + 2 NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
enzyme structure analysis
Prochlorococcus marinus
Synonyms
Synonyms
Commentary
Organism
cADO
-
Prochlorococcus marinus
cyanobacterial aldehyde-deformylating oxygenase
-
Prochlorococcus marinus
PMT_1231
-
Prochlorococcus marinus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Application (protein specific)
Application
Commentary
Organism
biofuel production
the conversion of long-chain fatty aldehydes to corresponding alkanes, that is catalyzed by cyanobacterial aldehyde-deformylating oxygenase (cADO), is probably useful for production of biofuel
Prochlorococcus marinus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
nonheme di-iron center
Prochlorococcus marinus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus MIT 9313
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
748032
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
C-H-bond-formation by enzyme cADO. The enzyme requires O2 to carry out the oxidative deformylation of substrate to form alkane and formate. The formate product derives an O atom from O2 and retains the aldehyde C-H bond, and the terminal methyl group of the alkane product incorporates an H atom from solvent
748032
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
748032
Prochlorococcus marinus
?
-
-
-
-
additional information
cyanobacterial aldehyde-deformylating oxygenase (cADO) converts long-chain fatty aldehydes to alkanes via a proposed diferric-peroxo intermediate that carries out the oxidative deformylation of the substrate. The synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal as substrate, detailed overview. Mechanistic studies suggest that the H atom donor can intercept the incipient alkyl radical formed in the oxidative deformylation step in competition with the oxygen rebound step typically used by most oxygenases for forming C-O bonds
748032
Prochlorococcus marinus MIT 9313
?
-
-
-
-
n-undecanal + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus
n-decane + formate + H2O + 2 NADP+
-
-
-
?
n-undecanal + O2 + 2 NADPH + 2 H+
-
748032
Prochlorococcus marinus MIT 9313
n-decane + formate + H2O + 2 NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
enzyme structure analysis
Prochlorococcus marinus
General Information
General Information
Commentary
Organism
evolution
structurally, the cADO enzyme belongs to the family of ferritin-like nonheme diiron-carboxylate enzymes that include methane monooxygenase (MMO), class I ribonucleotide reductase (RNR), and stearoyl-acyl carrier protein ?9-desaturase (DELTA9D), all of which share a common Fe2(His)2(O2CR)4 active site
Prochlorococcus marinus
additional information
the synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal with [FeIII(TMC)(delta2deltaO2)]+, detailed overview
Prochlorococcus marinus
General Information (protein specific)
General Information
Commentary
Organism
evolution
structurally, the cADO enzyme belongs to the family of ferritin-like nonheme diiron-carboxylate enzymes that include methane monooxygenase (MMO), class I ribonucleotide reductase (RNR), and stearoyl-acyl carrier protein ?9-desaturase (DELTA9D), all of which share a common Fe2(His)2(O2CR)4 active site
Prochlorococcus marinus
additional information
the synthetic iron(III)-peroxo complex [FeIII(eta2deltaO2)(TMC)]+ (TMC is tetramethylcyclam) causes a similar transformation in the presence of a suitable H atom donor, thus serving as a functional model for cADO, reaction analysis with undecanal with [FeIII(TMC)(delta2deltaO2)]+, detailed overview
Prochlorococcus marinus
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
Synonyms
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 = FACHB-805, Synechococcus elongatus PCC 7942 = FACHB-805 R2, Synechocystis sp. PCC 6803
BMC Biotechnol.
17
31-39
2017
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21
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28
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2
2
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9
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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
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4
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30
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746976
Park
Crystal structures of aldehyd ...
Limnothrix redekei, Limnothrix redekei KNUA012, Oscillatoria sp. KNUA011
Biochem. Biophys. Res. Commun.
477
395-400
2016
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2
2
2
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2
2
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2
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4
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747351
Bao
Structure-oriented substrate ...
Synechococcus elongatus PCC 7942 = FACHB-805, Synechococcus elongatus PCC 7942 = FACHB-805 R2
Biotechnol. Biofuels
9
185
2016
-
-
1
-
13
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7
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2
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6
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1
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14
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6
1
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8
1
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1
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1
1
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13
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7
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2
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1
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14
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1
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8
1
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2
2
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8
8
747353
Zhang
Microbial synthesis of propan ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
Biotechnol. Biofuels
9
80
2016
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1
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3
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2
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7
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4
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1
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1
1
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747081
Warui
Efficient delivery of long-ch ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
Biochemistry
54
1006-1015
2015
-
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2
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9
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2
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2
2
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748027
Rajakovich
Rapid reduction of the diferr ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
J. Am. Chem. Soc.
137
11695-11709
2015
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1
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8
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1
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1
1
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748032
Shokri
Conversion of aldehyde to alk ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
J. Am. Chem. Soc.
137
7686-7691
2015
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1
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2
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749051
Hayashi
Role of cysteine residues in ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
PLoS ONE
10
e0122217
2015
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1
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8
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3
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749212
Jia
Structural insights into the ...
Synechococcus elongatus PCC 7942 = FACHB-805, Synechococcus elongatus PCC 7942 = FACHB-805 R2
Protein Cell
6
55-67
2015
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3
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4
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726552
Das
Mechanistic insights from reac ...
Nostoc punctiforme
ACS Chem. Biol.
9
570-577
2014
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1
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746597
Buer
Insights into substrate and m ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Chem. Biol.
9
2584-2593
2014
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1
1
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2
2
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747074
Waugh
Solvent isotope effects on al ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
Biochemistry
53
5537-5543
2014
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1
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726548
Aukema
Cyanobacterial aldehyde deform ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Catal.
3
2228-2238
2013
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1
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-
727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus, Synechococcus elongatus PCC 7942
Biotechnol. Biofuels
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86
2013
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1
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4
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10
1
1
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1
1
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727312
Khara
Production of propane and othe ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
ChemBioChem
14
1204-1208
2013
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4
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8
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1
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1
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1
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727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
15801-15812
2013
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1
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1
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727693
Paul
Probing the mechanism of cyano ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
5234-5237
2013
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3
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1
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727001
Li
Evidence for only oxygenative ...
Prochlorococcus marinus
Biochemistry
51
7908-7916
2012
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1
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4
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3
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1
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1
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1
1
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715293
Warui
Detection of formate, rather t ...
Nostoc punctiforme
J. Am. Chem. Soc.
133
3316-3319
2011
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1
1
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715300
Li
Conversion of fatty aldehydes ...
Nostoc punctiforme
J. Am. Chem. Soc.
133
6158-6161
2011
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726957
Eser
Oxygen-independent alkane form ...
Nostoc punctiforme, Prochlorococcus marinus, Prochlorococcus marinus MIT9313, Synechococcus sp., Synechocystis sp.
Biochemistry
50
10743-10750
2011
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8
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15
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4
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4
4
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4
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15
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4
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4
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4
4
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713511
Schirmer
Microbial biosynthesis of alka ...
Nostoc punctiforme
Science
329
559-562
2010
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1
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3
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1
1
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648395
Schneider-Belhaddad
Solubilization, partial purifi ...
Pisum sativum
Arch. Biochem. Biophys.
377
341-349
2000
4
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7
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2
1
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1
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7
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1
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1
1
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648396
Kobayashi
Cobalt proteins ...
Botryococcus braunii
Eur. J. Biochem.
261
1-9
1999
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648394
Dennis
A cobalt-porphyrin enzyme conv ...
Botryococcus braunii, Botryococcus braunii Austin
Proc. Natl. Acad. Sci. USA
89
5306-5310
1992
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1
1
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648393
Dennis
Alkane biosynthesis by decarbo ...
Botryococcus braunii, Botryococcus braunii Austin
Arch. Biochem. Biophys.
287
268-275
1991
1
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5
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1
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648392
Cheesbrough
Microsomal preparation from an ...
Podiceps nigricollis
J. Biol. Chem.
263
2738-2743
1988
2
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1
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1
1
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648391
Cheesbrough
Alkane biosynthesis by decarbo ...
Pisum sativum
Proc. Natl. Acad. Sci. USA
81
6613-6617
1984
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