BRENDA - Enzyme Database show
show all sequences of 5.3.3.14

Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin

Guerra, D.J.; Browse, J.A.; Arch. Biochem. Biophys. 280, 336-345 (1990)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme activity depends more on acyl chain length than acyl carrier protein strucuture or origin
5819
Escherichia coli
?
-
-
-
-
trans-2-decenoyl-(acyl-carrier protein)
enzyme is equally active with acyl carrier protein derived from Escherichia coli, spinach or a protein A:acyl carrier protein fusion protein. With acyl carrier protein derived from Escherichia coli or from spinach, equilibrium results in equal amounts of trans-3- or cis-2-decenoyl-(acyl-carrier-protein), regardless of the initial substrate. With the fusion protein, yield is about 17% cis-3- and 49% trans-2-decenoyl-(acyl-carrier-protein)
5819
Escherichia coli
cis-3-decenoyl-(acyl-carrier protein)
-
-
-
r
trans-2-decenoyl-N-acetylcysteamine
-
5819
Escherichia coli
cis-3-decenoyl-N-acetylcysteamine
-
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme activity depends more on acyl chain length than acyl carrier protein strucuture or origin
5819
Escherichia coli
?
-
-
-
-
trans-2-decenoyl-(acyl-carrier protein)
enzyme is equally active with acyl carrier protein derived from Escherichia coli, spinach or a protein A:acyl carrier protein fusion protein. With acyl carrier protein derived from Escherichia coli or from spinach, equilibrium results in equal amounts of trans-3- or cis-2-decenoyl-(acyl-carrier-protein), regardless of the initial substrate. With the fusion protein, yield is about 17% cis-3- and 49% trans-2-decenoyl-(acyl-carrier-protein)
5819
Escherichia coli
cis-3-decenoyl-(acyl-carrier protein)
-
-
-
r
trans-2-decenoyl-N-acetylcysteamine
-
5819
Escherichia coli
cis-3-decenoyl-N-acetylcysteamine
-
-
-
r
Other publictions for EC 5.3.3.14
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)
665373
Fozo
The fabM gene product of Strep ...
Streptococcus mutans
J. Bacteriol.
186
4152-4158
2004
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1
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665480
Marrakchi
A new mechanism for anaerobic ...
Streptococcus pneumoniae
J. Biol. Chem.
277
44809-44816
2002
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2
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1
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666947
Leesong
Structure of a dehydratase-iso ...
Escherichia coli
Structure
4
253-264
1996
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5819
Guerra
Escherichia coli beta-hydroxyd ...
Escherichia coli
Arch. Biochem. Biophys.
280
336-345
1990
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3
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5814
Cronan
Derived amino acid sequence an ...
Escherichia coli
J. Biol. Chem.
263
4641-4646
1988
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1
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5808
Endo
Mode of inhibition of beta-hyd ...
Escherichia coli
J. Biol. Chem.
245
4293-4296
1970
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5803
Helmkamp
beta-Hydroxydecanoyl thioester ...
Escherichia coli
J. Biol. Chem.
244
6014-6022
1969
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1
1
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1
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1
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1
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5807
Helmkamp
beta-Hydroxydecanoyl thioester ...
Escherichia coli
J. Biol. Chem.
243
3229-3231
1968
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5
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4
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5
4
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665451
Rando
Mechanism of action of beta-hy ...
Escherichia coli
J. Biol. Chem.
243
5627-5634
1968
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1
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1
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5800
Kass
beta-Hydroxydecanoyl thioester ...
Escherichia coli
J. Biol. Chem.
242
4418-4431
1967
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2
1
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2
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1
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