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EC Tree
IUBMB Comments While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs . ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
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a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
the reactions of EC 4.2.1.60 and EC 5.3.3.14 are carried out by the same active site carrying a His and a Asp residue in a hydrophobic environment
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a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
reaction of EC4.2.1.60 and isomerization reaction, both catalyzed by the enzyme, share the common intermediate, enzyme-bound alpha,beta-decenoate
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decenoyl-[acyl-carrier protein] Delta2-trans-Delta3-cis-isomerase
While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
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cis-3-decenoyl-N-acetylcysteamine
trans-2-decenoyl-N-acetylcysteamine
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r
cis-beta,gamma-decenoyl-N-acetylcysteamine
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trans-2-decenoyl-(acyl-carrier protein)
cis-3-decenoyl-(acyl-carrier protein)
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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)
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r
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
trans-2-octenoyl-N-acetylcysteamine
cis-3-octenoyl-N-acetylcysteamine
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?
additional information
?
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trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
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r
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
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?
additional information
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enzyme activity depends more on acyl chain length than acyl carrier protein strucuture or origin
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?
additional information
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enzyme does not catalyze dehydration reaction of EC 4.2.1.60
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3-decynoyl-N-acetylcysteamine
3-dodecynoyl-N-acetylcysteamine
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3-nonynoyl-N-acetylcysteamine
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noncompetitive
3-octynoyl-N-acetylcysteamine
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24% inhibition at 0.005 mM
3-undecynoyl-N-acetylcysteamine
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p-chloromercuribenzoate
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0.5 mM, 35% inhibition
additional information
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not inhibitory: iodoacetic acid, chloroacetic acid, iodoacetamide, N-ethylmaleimide
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3-decynoyl-N-acetylcysteamine
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covalent modification of ative site residue H70
3-decynoyl-N-acetylcysteamine
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strong inhibition of both dehydrase activity of EC 4.2.1.60 and isomerase activity of enzyme
3-decynoyl-N-acetylcysteamine
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irreversible inactivation of both dehydrase activity of EC 4.2.1.60 and isomerase activity of enzyme, inhibition occurs through isomerization to the allene and subsequent covalent modification of enzyme
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0.5
cis-beta,gamma-Decenoyl-N-acetylcysteamine
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pH 7.0
additional information
additional information
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Km-value gradually decreases with decreasing pH-value
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15
cis-3-decenoyl-N-acetylcysteamine
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pH 9.0, 30°C
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0.00013
3-decynoyl-N-acetylcysteamine
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pH 7.0, 30°C, isomerase acitivity
0.00075
3-dodecynoyl-N-acetylcysteamine
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pH 7.0, 30°C, isomerase acitivity
0.00023
3-nonynoyl-N-acetylcysteamine
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pH 7.0, 30°C, isomerase acitivity
0.00019
3-undecynoyl-N-acetylcysteamine
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pH 7.0, 30°C, isomerase acitivity
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additional information
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direct assay for enzyme activity based on substrate analogues
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7.3 - 10.2
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more than 50% of activity maximum within this range
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brenda
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brenda
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
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brenda
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
Swissprot
brenda
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
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brenda
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18000
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2 * 18000, SDS-PAGE
18800
x * 18800, calculated
27500
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sucrose density sedimentation
31000
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4 * 31000, SDS-PAGE
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tetramer
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4 * 31000, SDS-PAGE
dimer
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2 * 18000, SDS-PAGE
dimer
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crystallization data
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free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine
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additional information
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enzyme insertion mutant, no production of unsaturated fatty acids by mutant strain. Strain is extremely sensitive to low pH-values and exhibits reduced glycolyic capability and altered membrane composition, resulting in higher impermeability to protons
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simplified purification protocol
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Kass, L.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
242
4418-4431
1967
Escherichia coli
brenda
Helmkamp, G.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site
J. Biol. Chem.
244
6014-6022
1969
Escherichia coli
brenda
Helmkamp, G.; Rando, R.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
3229-3231
1968
Escherichia coli
brenda
Endo, K.; Helmkamp, G.M.; Bloch, K.
Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine
J. Biol. Chem.
245
4293-4296
1970
Escherichia coli
brenda
Cronan, J.E.; Li, W.B.; Coleman, R.; Narasimhan, M.; De Mendoza, D.; Schwab, J.M.
Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
263
4641-4646
1988
Escherichia coli (P0A6Q3)
brenda
Guerra, D.J.; Browse, J.A.
Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin
Arch. Biochem. Biophys.
280
336-345
1990
Escherichia coli
brenda
Fozo, E.M.; Quivey, R.G., Jr.
The fabM gene product of Streptococcus mutans is responsible for the synthesis of monounsaturated fatty acids and is necessary for survival at low pH
J. Bacteriol.
186
4152-4158
2004
Streptococcus mutans
brenda
Rando, R.R.; Bloch, K.
Mechanism of action of beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
5627-5634
1968
Escherichia coli
brenda
Marrakchi, H.; Choi, K.H.; Rock, C.O.
A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae
J. Biol. Chem.
277
44809-44816
2002
Streptococcus pneumoniae
brenda
Leesong, M.; Henderson, B.S.; Gillig, J.R.; Schwab, J.M.; Smith, J.L.
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site
Structure
4
253-264
1996
Escherichia coli
brenda
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5.3.3.14 trans-2-decenoyl-[acyl-carrier protein] isomerase
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