We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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]
-
-
-
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cis-3-decenoyl-N-acetylcysteamine
trans-2-decenoyl-N-acetylcysteamine
-
-
-
-
r
cis-beta,gamma-decenoyl-N-acetylcysteamine
?
-
-
-
-
?
trans-2-decenoyl-(acyl-carrier protein)
cis-3-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)
-
-
r
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
trans-2-octenoyl-N-acetylcysteamine
cis-3-octenoyl-N-acetylcysteamine
-
-
-
-
?
additional information
?
-
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
-
-
-
-
r
trans-2-decenoyl-N-acetylcysteamine
cis-3-decenoyl-N-acetylcysteamine
-
-
-
-
?
additional information
?
-
-
enzyme activity depends more on acyl chain length than acyl carrier protein strucuture or origin
-
-
?
additional information
?
-
-
enzyme does not catalyze dehydration reaction of EC 4.2.1.60
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-decynoyl-N-acetylcysteamine
3-dodecynoyl-N-acetylcysteamine
-
-
3-nonynoyl-N-acetylcysteamine
-
noncompetitive
3-octynoyl-N-acetylcysteamine
-
24% inhibition at 0.005 mM
3-undecynoyl-N-acetylcysteamine
-
-
p-chloromercuribenzoate
-
0.5 mM, 35% inhibition
additional information
-
not inhibitory: iodoacetic acid, chloroacetic acid, iodoacetamide, N-ethylmaleimide
-
3-decynoyl-N-acetylcysteamine
-
covalent modification of ative site residue H70
3-decynoyl-N-acetylcysteamine
-
strong inhibition of both dehydrase activity of EC 4.2.1.60 and isomerase activity of enzyme
3-decynoyl-N-acetylcysteamine
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.5
cis-beta,gamma-Decenoyl-N-acetylcysteamine
-
pH 7.0
additional information
additional information
-
Km-value gradually decreases with decreasing pH-value
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15
cis-3-decenoyl-N-acetylcysteamine
-
pH 9.0, 30ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00013
3-decynoyl-N-acetylcysteamine
-
pH 7.0, 30ưC, isomerase acitivity
0.00075
3-dodecynoyl-N-acetylcysteamine
-
pH 7.0, 30ưC, isomerase acitivity
0.00023
3-nonynoyl-N-acetylcysteamine
-
pH 7.0, 30ưC, isomerase acitivity
0.00019
3-undecynoyl-N-acetylcysteamine
-
pH 7.0, 30ưC, isomerase acitivity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
direct assay for enzyme activity based on substrate analogues
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.3 - 10.2
-
more than 50% of activity maximum within this range
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60
-
-
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
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
18000
-
2 * 18000, SDS-PAGE
18800
x * 18800, calculated
27500
-
sucrose density sedimentation
31000
-
4 * 31000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
tetramer
-
4 * 31000, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
dimer
-
crystallization data
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
simplified purification protocol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
html completed