BRENDA - Enzyme Database
show all sequences of 4.1.99.5

Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound

Buer, B.C.; Paul, B.; Das, D.; Stuckey, J.A.; Marsh, E.N.; ACS Chem. Biol. 9, 2584-2593 (2014)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant wild-type and mutant L194A in complex with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal, trans-2-nonylcyclopropane-1-carboxylic acid, or stearate, X-ray diffraction structure determination and analysis at 1.60-2.21 A resolution. It appears that the fatty acids are necessary for crystallization. Attempts to crystallize the enzyme in fully metalated form by including Fe2+ or Zn2+ ions in the crystallization buffer together with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal are unsuccessful
Prochlorococcus marinus
Engineering
Protein Variants
Commentary
Organism
L194A
site-directed mutagenesis, the mutant has kinetic properties very similar to the wild-type enzyme
Prochlorococcus marinus
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
substrate inhibition might occur with short aldehydes if a second substrate molecule is bound in the channel preventing product release
Prochlorococcus marinus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
a nonheme di-iron enzyme
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+
the aldehyde proton is retained in formate and one of the oxygen atoms derives from molecular oxygen, whereas the proton in the product alkane derives from the solvent. Initial formation of a diferric intermediate in the cADO catalyzed reaction. Addition of a further electron to this complex is proposed to lead to its breakdown and scission of the C1-C2 bond. A radical mechanism for C1-C2 bond cleavage is supported by the observed ring-opening of cyclopropyl aldehydes and oxiranyl aldehydes designed to act as radical clocks during deformylation by cADO. Structure-function analysis
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+
-
746597
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
NMR studies of substrate Binding to cADO
746597
Prochlorococcus marinus
?
-
-
-
-
additional information
NMR studies of substrate Binding to cADO
746597
Prochlorococcus marinus MIT 9313
?
-
-
-
-
n-octadecanal + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus MIT 9313
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
746597
Prochlorococcus marinus
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
746597
Prochlorococcus marinus MIT 9313
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
aldehyde decarbonylase
-
Prochlorococcus marinus
cADO
-
Prochlorococcus marinus
cyanobacterial aldehyde deformylating oxygenase
-
Prochlorococcus marinus
PMT_1231
-
Prochlorococcus marinus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
low rates of turnover are measured for cADO
Prochlorococcus marinus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant wild-type and mutant L194A in complex with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal, trans-2-nonylcyclopropane-1-carboxylic acid, or stearate, X-ray diffraction structure determination and analysis at 1.60-2.21 A resolution. It appears that the fatty acids are necessary for crystallization. Attempts to crystallize the enzyme in fully metalated form by including Fe2+ or Zn2+ ions in the crystallization buffer together with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal are unsuccessful
Prochlorococcus marinus
Engineering (protein specific)
Protein Variants
Commentary
Organism
L194A
site-directed mutagenesis, the mutant has kinetic properties very similar to the wild-type enzyme
Prochlorococcus marinus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
substrate inhibition might occur with short aldehydes if a second substrate molecule is bound in the channel preventing product release
Prochlorococcus marinus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
a nonheme di-iron enzyme
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+
-
746597
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
additional information
NMR studies of substrate Binding to cADO
746597
Prochlorococcus marinus
?
-
-
-
-
additional information
NMR studies of substrate Binding to cADO
746597
Prochlorococcus marinus MIT 9313
?
-
-
-
-
n-octadecanal + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octadecanal + O2 + 2 NADPH + 2 H+
-
746597
Prochlorococcus marinus MIT 9313
heptadecane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
746597
Prochlorococcus marinus
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
n-octanal + O2 + 2 NADPH + 2 H+
binding of 1-[13C]-octanal to enzyme cADO is monitored by 13C NMR
746597
Prochlorococcus marinus MIT 9313
n-heptane + formate + H2O + 2 NADP+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
low rates of turnover are measured for cADO
Prochlorococcus marinus
General Information
General Information
Commentary
Organism
additional information
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview
Prochlorococcus marinus
physiological function
the nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the deformylation of aliphatic aldehydes to alkanes and formate
Prochlorococcus marinus
General Information (protein specific)
General Information
Commentary
Organism
additional information
residue L194, at the center of the hydrophobic cavity, might serve as a gateway for substrate entry, but L194 does not play a kinetically significant role in limiting substrate access to the active site. Structure of metal-free cADO, overview
Prochlorococcus marinus
physiological function
the nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the deformylation of aliphatic aldehydes to alkanes and formate
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
-
-
-
-
21
-
-
8
-
2
-
3
-
9
-
-
-
-
-
-
-
-
11
1
7
-
-
-
28
-
-
-
1
-
-
-
-
-
-
1
-
21
-
-
-
-
8
-
2
-
3
-
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-
-
-
-
-
-
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
-
14
-
-
-
-
-
-
-
4
-
-
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4
4
-
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
-
5
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-
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6
2
4
2
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2
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2
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2
2
2
2
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3
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6
2
2
-
-
-
2
-
-
-
-
4
4
-
-
-
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
-
-
7
-
-
-
2
-
6
-
-
1
-
-
-
-
-
14
-
6
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
-
3
1
-
-
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1
-
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1
1
-
3
-
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-
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
-
2
-
-
-
-
-
-
-
1
-
-
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-
1
-
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-
-
-
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-
2
-
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-
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-
-
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
-
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1
-
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10
-
2
1
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1
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2
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-
2
-
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-
-
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1
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2
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-
-
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
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2
-
6
-
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1
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8
1
3
-
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1
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1
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1
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1
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2
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8
1
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-
-
-
-
-
-
2
2
-
-
-
749051
Hayashi
Role of cysteine residues in ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
PLoS ONE
10
e0122217
2015
-
-
1
-
8
-
-
1
-
1
-
2
-
7
-
-
1
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-
-
-
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10
-
2
1
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5
-
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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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1
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2
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1
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10
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1
-
5
-
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-
-
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3
3
-
-
-
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
-
-
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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6
1
5
1
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1
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1
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1
1
1
3
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1
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1
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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
-
-
1
-
-
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1
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1
-
1
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2
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1
1
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6
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3
1
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3
1
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2
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1
2
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1
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1
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1
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1
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6
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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
-
-
-
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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4
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1
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1
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1
1
1
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1
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1
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2
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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
-
-
1
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-
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1
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1
-
2
1
3
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1
1
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6
-
2
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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1
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2
1
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1
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6
-
1
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1
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-
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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
-
-
1
-
-
-
-
-
-
-
-
-
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6
-
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1
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-
-
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8
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3
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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8
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1
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1
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727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus, Synechococcus elongatus PCC 7942
Biotechnol. Biofuels
6
86
2013
-
-
1
-
-
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-
1
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1
2
-
4
-
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1
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-
-
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10
1
3
1
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1
1
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3
-
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1
3
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1
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1
2
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1
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10
1
1
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1
1
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-
-
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-
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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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727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
15801-15812
2013
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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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727001
Li
Evidence for only oxygenative ...
Prochlorococcus marinus
Biochemistry
51
7908-7916
2012
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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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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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15
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713511
Schirmer
Microbial biosynthesis of alka ...
Nostoc punctiforme
Science
329
559-562
2010
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648395
Schneider-Belhaddad
Solubilization, partial purifi ...
Pisum sativum
Arch. Biochem. Biophys.
377
341-349
2000
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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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648393
Dennis
Alkane biosynthesis by decarbo ...
Botryococcus braunii, Botryococcus braunii Austin
Arch. Biochem. Biophys.
287
268-275
1991
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-
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-
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648392
Cheesbrough
Microsomal preparation from an ...
Podiceps nigricollis
J. Biol. Chem.
263
2738-2743
1988
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-
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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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