Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I and Organism(s) Homo sapiens and UniProt Accession Q9NWU1

for references in articles please use BRENDA:EC2.3.1.41
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) . The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9NWU1
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
condensing enzyme, beta-ketoacyl synthase, kas i, beta-ketoacyl-acp synthase, beta-ketoacyl synthetase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acp synthase, beta-ketoacyl-acp synthase i, beta-ketoacyl-acyl carrier protein synthase i, fatty acid condensing enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-ketoacyl [ACP] synthase
-
beta-ketoacyl-ACP synthase
-
3-ketoacyl-acyl carrier protein synthase
-
-
-
-
3-oxoacyl-[acyl-carrier-protein] synthase
-
-
-
-
acyl-malonyl(acyl-carrier-protein)-condensing enzyme
-
-
-
-
beta-ketoacyl acyl carrier protein synthase
-
-
-
-
beta-ketoacyl synthetase
-
-
-
-
beta-ketoacyl-ACP synthetase
-
-
-
-
beta-ketoacyl-acyl carrier protein synthetase
-
-
-
-
beta-ketoacyl-[acyl carrier protein] synthase
-
-
-
-
beta-ketoacylsynthase
-
-
-
-
condensing enzyme
-
-
-
-
fatty acid condensing enzyme
-
-
-
-
synthase, 3-oxoacyl-[acyl-carrier-protein]
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
structure-activity analysis, reaction mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
9077-10-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
butanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
important role in generation of the lipoic acid precursor octanoyl-acyl-carrier protein
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cerulenin
-
cerulenin
-
50% inhibition at 0.2 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
acetyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0039
butanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0018
decanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0095
dodecanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0019
hexanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0508
myristoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0109
octanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.2
butanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
551
decanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
303
dodecanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
353
hexanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
6
myristoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
66
octanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low level
Manually annotated by BRENDA team
-
most abundant
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
-
most abundant
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OXSM_HUMAN
459
0
48843
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45800
-
x * 45800, SDS-PAGE, recombinant protein without N-terminal targeting sequence, with His-tag
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
secondary structure, a dimer with an alpha-beta-alpha-beta-alpha-thiolase fold capped by an alpha-helical region connecting the strands of the N-terminal beta-sheet, crystal structure analysis
?
-
x * 45800, SDS-PAGE, recombinant protein without N-terminal targeting sequence, with His-tag
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
mitochondrial targeting sequence of 38 residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or complexed with acyl-CoA, hanging drop vapour diffusion method, 0.002 ml of protein solution, containing 0.087 mg of protein with or without 4 mM hexanoyl-CoA, mixed with 0.002 ml of reservoir solution containing 24% w/v PEG 3350 and 0.2 M NH4Cl, 5-8 days at room temperature, rod-shaped single crystals, X-ray diffraction structure determination and analysis at 1.6 A resolution, structure modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strains XL-1 blue and M15
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme in Escherichia coli strains XL-1 blue and M15
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for antibacterial drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, L.; Joshi, A.K.; Hofmann, J.; Schweizer, E.; Smith, S.
Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain
J. Biol. Chem.
280
12422-12429
2005
Homo sapiens
Manually annotated by BRENDA team
Christensen, C.E.; Kragelund, B.B.; von Wettstein-Knowles, P.; Henriksen, A.
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase
Protein Sci.
16
261-272
2007
Homo sapiens (Q9NWU1), Homo sapiens
Manually annotated by BRENDA team