BRENDA - Enzyme Database show
show all sequences of 4.1.99.5

Crystal structures of aldehyde deformylating oxygenase from Limnothrix sp. KNUA012 and Oscillatoria sp. KNUA011

Park, A.K.; Kim, I.S.; Jeon, B.W.; Roh, S.J.; Ryu, M.Y.; Baek, H.R.; Jo, S.W.; Kim, Y.S.; Park, H.; Lee, J.H.; Yoon, H.S.; Kim, H.W.; Biochem. Biophys. Res. Commun. 477, 395-400 (2016)

Data extracted from this reference:

Application
Application
Commentary
Organism
biofuel production
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo
Limnothrix redekei
biofuel production
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo
Oscillatoria sp. KNUA011
Cloned(Commentary)
Commentary
Organism
sequence comparisons
Limnothrix redekei
sequence comparisons
Oscillatoria sp. KNUA011
Crystallization (Commentary)
Crystallization
Organism
crystal structure determination and analysis
Limnothrix redekei
crystal structure determination and analysis
Oscillatoria sp. KNUA011
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Limnothrix redekei
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Oscillatoria sp. KNUA011
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Limnothrix redekei KNUA012
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Limnothrix redekei
A0A191T893
-
-
Limnothrix redekei KNUA012
A0A191T893
-
-
Oscillatoria sp. KNUA011
A0A191T887
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Limnothrix redekei
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Oscillatoria sp. KNUA011
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Limnothrix redekei KNUA012
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
substrate binding site analysis
746976
Limnothrix redekei
?
-
-
-
-
additional information
substrate binding site analysis
746976
Oscillatoria sp. KNUA011
?
-
-
-
-
additional information
substrate binding site analysis
746976
Limnothrix redekei KNUA012
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
secondary structure element analysis. The LiADO structure resembles ADO structures with an empty active site
Limnothrix redekei
More
secondary structure element analysis. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate
Oscillatoria sp. KNUA011
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Limnothrix redekei
37
-
assay at
Oscillatoria sp. KNUA011
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Limnothrix redekei
7.4
-
assay at
Oscillatoria sp. KNUA011
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Limnothrix redekei
NADPH
-
Oscillatoria sp. KNUA011
Application (protein specific)
Application
Commentary
Organism
biofuel production
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo
Limnothrix redekei
biofuel production
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo
Oscillatoria sp. KNUA011
Cloned(Commentary) (protein specific)
Commentary
Organism
sequence comparisons
Limnothrix redekei
sequence comparisons
Oscillatoria sp. KNUA011
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Limnothrix redekei
NADPH
-
Oscillatoria sp. KNUA011
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure determination and analysis
Limnothrix redekei
crystal structure determination and analysis
Oscillatoria sp. KNUA011
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Limnothrix redekei
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Oscillatoria sp. KNUA011
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Limnothrix redekei KNUA012
-
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
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Limnothrix redekei
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Oscillatoria sp. KNUA011
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746976
Limnothrix redekei KNUA012
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
substrate binding site analysis
746976
Limnothrix redekei
?
-
-
-
-
additional information
substrate binding site analysis
746976
Oscillatoria sp. KNUA011
?
-
-
-
-
additional information
substrate binding site analysis
746976
Limnothrix redekei KNUA012
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
secondary structure element analysis. The LiADO structure resembles ADO structures with an empty active site
Limnothrix redekei
More
secondary structure element analysis. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate
Oscillatoria sp. KNUA011
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Limnothrix redekei
37
-
assay at
Oscillatoria sp. KNUA011
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Limnothrix redekei
7.4
-
assay at
Oscillatoria sp. KNUA011
General Information
General Information
Commentary
Organism
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution
Limnothrix redekei
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix
Oscillatoria sp. KNUA011
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
Limnothrix redekei
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
Oscillatoria sp. KNUA011
General Information (protein specific)
General Information
Commentary
Organism
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. The LiADO structure resembles ADO structures with an empty active site, the LiADO active site is vacant of iron and substrates, helix 5 of LiADO, which lacks iron in the active site, presents two conformations (one long and two short helices), indicating that an equilibrium exists between the two states in solution
Limnothrix redekei
additional information
the enzyme structure consists of eight a-helices found in ferritin-like di-iron proteins. Residues Tyr21, Ile27, Val28, Phe67, Phe86, Phe87, Phe117, Ala118, Ala121, Tyr122, Try125, and Tyr184 contributing to substrate binding, and Glu32, Glu60, His63, Glu115, Glu144, and His147 participating in iron coordination. OsADO structure resembles ADO structures with active sites containing both metal co-factor and substrate, OsADO active site is fully occupied, helix 5 of OsADO with an iron bound in the active site is a long helix
Oscillatoria sp. KNUA011
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
Limnothrix redekei
physiological function
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis
Oscillatoria sp. KNUA011
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
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-
-
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21
-
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8
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2
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3
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9
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11
1
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28
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21
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11
1
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28
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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
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4
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5
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6
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13
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30
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4
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4
4
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5
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6
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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
-
2
2
2
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3
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5
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2
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2
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6
2
2
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2
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4
4
-
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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
-
-
-
-
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14
-
1
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8
1
-
-
1
-
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-
1
1
-
13
-
-
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7
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2
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1
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14
-
1
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-
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
-
-
-
-
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2
-
7
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4
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1
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1
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1
1
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3
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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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1
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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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2
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8
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1
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10
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1
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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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1
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2
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6
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1
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2
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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1
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1
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2
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7
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1
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10
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5
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1
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1
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8
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10
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1
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5
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3
3
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749212
Jia
Structural insights into the ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Protein Cell
6
55-67
2015
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1
1
3
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1
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2
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6
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1
1
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1
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3
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6
1
1
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1
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4
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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1
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1
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1
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1
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1
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3
1
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1
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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1
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1
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2
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6
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1
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8
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1
1
1
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1
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8
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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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1
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1
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2
1
3
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1
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6
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1
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1
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1
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1
1
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1
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2
1
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1
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6
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1
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1
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1
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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6
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1
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8
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1
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1
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1
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1
1
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8
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1
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727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus
Biotechnol. Biofuels
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2013
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1
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727312
Khara
Production of propane and othe ...
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8
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1
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727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
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2013
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1
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727693
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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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7908-7916
2012
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1
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1
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715293
Warui
Detection of formate, rather t ...
Nostoc punctiforme
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3316-3319
2011
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1
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715300
Li
Conversion of fatty aldehydes ...
Nostoc punctiforme
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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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15
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4
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4
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4
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713511
Schirmer
Microbial biosynthesis of alka ...
Nostoc punctiforme
Science
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2010
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1
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Schneider-Belhaddad
Solubilization, partial purifi ...
Pisum sativum
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341-349
2000
4
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1
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1
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648396
Kobayashi
Cobalt proteins ...
Botryococcus braunii
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1-9
1999
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648394
Dennis
A cobalt-porphyrin enzyme conv ...
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5306-5310
1992
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Dennis
Alkane biosynthesis by decarbo ...
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268-275
1991
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Cheesbrough
Microsomal preparation from an ...
Podiceps nigricollis
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648391
Cheesbrough
Alkane biosynthesis by decarbo ...
Pisum sativum
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1984
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