BRENDA - Enzyme Database show
show all sequences of 1.2.1.50

A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol

Hofvander, P.; Doan, T.T.; Hamberg, M.; FEBS Lett. 585, 3538-3543 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
plasmid pHisMBPMarFAR harbouring the sequence of hypothetical protein Maqu_2220 added by His-tag and maltose binding protein transformed to Escherichia coli strain Rosetta (DE3) for heterologous protein expression
Marinobacter hydrocarbonoclasticus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Marinobacter hydrocarbonoclasticus
-
-
-
Purification (Commentary)
Commentary
Organism
via fusion protein with maltose binding protein and an N-terminal His-tag fusion
Marinobacter hydrocarbonoclasticus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0273
-
ricinoleoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.043
-
palmitoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.0677
-
stearoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.0774
-
icosanoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.1082
-
oleoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
erucoyl-CoA + NADPH + H+
erucoyl-CoA i.e. (13Z)-docos-13-enoyl-CoA
725007
Marinobacter hydrocarbonoclasticus
(13Z)-docos-13-enal + CoA + NADP+
further direct reduction of (13Z)-docos-13-enal into the corresponding (13Z)-docos-13-en-1-ol
-
-
?
icosanoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
icosanal + CoA + NADP+
further direct reduction of icosanal into the corresponding icosan-1-ol
-
-
?
additional information
in contrast to other prokaryotes, the enzyme performs the two reduction steps from acyl-CoA to fatty alcohol in a single step which is typical for eukaryotes
725007
Marinobacter hydrocarbonoclasticus
?
-
-
-
?
additional information
shorter acyl chains than 16 carbon are less effectively utilized and with these substrates substantial amounts of both free fatty acids and fatty aldehyde are formed
725007
Marinobacter hydrocarbonoclasticus
?
-
-
-
?
oleoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
(9Z)-octadec-9-enal + CoA + NADP+
further direct reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
-
-
?
palmitoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
hexadecanal + CoA + NADP+
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
-
?
palmitoyl-[acyl-carrier protein] + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
hexadecanal + [acyl-carrier protein] + NADP+
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
-
?
ricinoleoyl-CoA + NADPH + H+
ricinoleoyl-CoA i.e. (9Z,12R)-12-hydroxyoctadec-9-enoyl-CoA
725007
Marinobacter hydrocarbonoclasticus
(9Z,12R)-12-hydroxyoctadec-9-enal + CoA + NADP+
further direct reduction of (9Z,12R)-12-hydroxyoctadec-9-enal into the corresponding (9Z,12R)-octadec-9-ene-1,12-diol
-
-
?
stearoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
octadecanal + CoA + NADP+
further direct reduction of octadecanal into the corresponding octadecan-1-ol
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
plasmid pHisMBPMarFAR harbouring the sequence of hypothetical protein Maqu_2220 added by His-tag and maltose binding protein transformed to Escherichia coli strain Rosetta (DE3) for heterologous protein expression
Marinobacter hydrocarbonoclasticus
Purification (Commentary) (protein specific)
Commentary
Organism
via fusion protein with maltose binding protein and an N-terminal His-tag fusion
Marinobacter hydrocarbonoclasticus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0273
-
ricinoleoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.043
-
palmitoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.0677
-
stearoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.0774
-
icosanoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
0.1082
-
oleoyl-CoA, pH 7.0, 30°C
Marinobacter hydrocarbonoclasticus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
erucoyl-CoA + NADPH + H+
erucoyl-CoA i.e. (13Z)-docos-13-enoyl-CoA
725007
Marinobacter hydrocarbonoclasticus
(13Z)-docos-13-enal + CoA + NADP+
further direct reduction of (13Z)-docos-13-enal into the corresponding (13Z)-docos-13-en-1-ol
-
-
?
icosanoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
icosanal + CoA + NADP+
further direct reduction of icosanal into the corresponding icosan-1-ol
-
-
?
additional information
in contrast to other prokaryotes, the enzyme performs the two reduction steps from acyl-CoA to fatty alcohol in a single step which is typical for eukaryotes
725007
Marinobacter hydrocarbonoclasticus
?
-
-
-
?
additional information
shorter acyl chains than 16 carbon are less effectively utilized and with these substrates substantial amounts of both free fatty acids and fatty aldehyde are formed
725007
Marinobacter hydrocarbonoclasticus
?
-
-
-
?
oleoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
(9Z)-octadec-9-enal + CoA + NADP+
further direct reduction of (9Z)-octadec-9-enal into the corresponding (9Z)-octadec-9-en-1-ol
-
-
?
palmitoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
hexadecanal + CoA + NADP+
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
-
?
palmitoyl-[acyl-carrier protein] + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
hexadecanal + [acyl-carrier protein] + NADP+
further direct reduction of hexadecanal into the corresponding hexadecan-1-ol
-
-
?
ricinoleoyl-CoA + NADPH + H+
ricinoleoyl-CoA i.e. (9Z,12R)-12-hydroxyoctadec-9-enoyl-CoA
725007
Marinobacter hydrocarbonoclasticus
(9Z,12R)-12-hydroxyoctadec-9-enal + CoA + NADP+
further direct reduction of (9Z,12R)-12-hydroxyoctadec-9-enal into the corresponding (9Z,12R)-octadec-9-ene-1,12-diol
-
-
?
stearoyl-CoA + NADPH + H+
-
725007
Marinobacter hydrocarbonoclasticus
octadecanal + CoA + NADP+
further direct reduction of octadecanal into the corresponding octadecan-1-ol
-
-
?
Other publictions for EC 1.2.1.50
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)
724299
Willis
Characterization of a fatty ac ...
Marinobacter hydrocarbonoclasticus
Biochemistry
50
10550-10558
2011
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10
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725007
Hofvander
A prokaryotic acyl-CoA reducta ...
Marinobacter hydrocarbonoclasticus
FEBS Lett.
585
3538-3543
2011
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724655
Zhu
The reductase domain in a Type ...
Cryptosporidium parvum
BMC Biochem.
11
46
2010
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725132
Teerawanichpan
A fatty acyl-CoA reductase hig ...
Apis mellifera
Insect Biochem. Mol. Biol.
40
641-649
2010
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1
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1
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7
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2
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699807
Doan
Functional expression of five ...
Arabidopsis thaliana
J. Plant Physiol.
166
787-796
2009
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1
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5
5
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5
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3
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5
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5
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5
5
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15
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5
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671446
Kalscheuer
Neutral lipid biosynthesis in ...
Simmondsia chinensis
Appl. Environ. Microbiol.
72
1373-1379
2006
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1
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288215
Ishige
Wax ester production from n-al ...
Acinetobacter sp., Acinetobacter sp. M-1
Appl. Environ. Microbiol.
68
1192-1195
2002
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1
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6
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12
2
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12
2
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288216
Metz
Purification of a jojoba embry ...
Simmondsia chinensis
Plant Physiol.
122
635-644
2000
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288212
Lee
Cysteine-286 as the site of ac ...
Photobacterium leiognathi, Photobacterium phosphoreum
Biochim. Biophys. Acta
1338
215-222
1997
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2
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6
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6
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288213
Vioque
Resolution and purification of ...
Pisum sativum
Arch. Biochem. Biophys.
340
64-72
1997
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288211
Wang
Solubilization, purification a ...
Anas platyrhynchos
Biochem. Biophys. Res. Commun.
208
210-215
1995
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288265
Wall
Covalent reaction of cerulenin ...
Photobacterium phosphoreum
Biochem. Cell Biol.
67
163-167
1989
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666
Rodriguez
-
Different sites for fatty acid ...
Photobacterium phosphoreum
Biochim. Biophys. Acta
964
266-275
1988
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662
Wall
-
Subunit structure of the fatty ...
Photobacterium phosphoreum
Biochemistry
25
4315-4321
1986
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288268
Rodriguez
-
Fatty acid reductase from Phot ...
Photobacterium phosphoreum
Methods Enzymol.
133
172-182
1986
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288269
Wall
Intersubunit transfer of fatty ...
Photobacterium phosphoreum
J. Biol. Chem.
261
15981-15988
1986
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288270
Rodriguez
Purification of the acyl coenz ...
Photobacterium phosphoreum
J. Biol. Chem.
258
5233-5237
1983
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665
Riendeau
Resolution of the fatty acid r ...
Photobacterium phosphoreum
J. Biol. Chem.
257
6908-6915
1982
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288272
Riendeau
Fatty acid reductase in biolum ...
Photobacterium phosphoreum
Can. J. Biochem.
59
440-446
1981
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