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Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I and Organism(s) Arabidopsis thaliana and UniProt Accession Q8L3X9
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2.3.1.41 beta-ketoacyl-[acyl-carrier-protein] synthase IIUBMB 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].
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Word Map
- 2.3.1.41
- polyketide
- cerulenin
- malonyl-coa
-
thioesterase
- elongase
-
enoyl
- thiolactomycin
-
transacylase
-
mycolic
- malonyl-acp
- acyl-acps
-
very-long-chain
-
dehydrase
- 4'-phosphopantetheine
- cuphea
-
vlcfas
-
cis-vaccenic
-
malonyl-coa:acp
-
actinorhodin
- platensimycin
- acetyl-acp
- drug development
-
6-methylsalicylic
- 3-oxoacyl-acps
-
claisen
- pharmacology
- nutrition
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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, oskasi, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl-acyl carrier protein synthase
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-
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3-oxoacyl-[acyl-carrier-protein] synthase
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-
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acyl-malonyl(acyl-carrier-protein)-condensing enzyme
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beta-ketoacyl acyl carrier protein synthase
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beta-ketoacyl synthetase
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beta-ketoacyl-ACP synthetase
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beta-ketoacyl-acyl carrier protein synthetase
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beta-ketoacyl-[acyl carrier protein] synthase
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beta-ketoacylsynthase
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condensing enzyme
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fatty acid condensing enzyme
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synthase, 3-oxoacyl-[acyl-carrier-protein]
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
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-
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
9077-10-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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?
additional information
?
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no substrate: acetyl-[acyl-carrier protein]
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?
additional information
?
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no substrate: acetyl-[acyl-carrier protein]
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20°C for one or several weeks, enzyme synthesizes predominantly C8 acyl chains
additional information
-
enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20°C for one or several weeks, enzyme synthesizes predominantly C8 acyl chains
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
also found in 7-d-old seedling, root, flower, young silique, embryos at late cotyledon stage and stalk
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
crucial for fatty acid synthesis, deficiency results in semidwarf and variegated leaves, in a mutant chloroplast division is arrested at early developmental stages of rosette leaves
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KASM_ARATH
461
0
49379
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
20 amino acid mitochondrial targeting sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, unstable in crude extracts lacking glycerol. Enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20°C for one or several weeks, enzyme synthesizes predominantly C8 acyl chains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olsen, J.G.; Rasmussen, A.V.; von Wettstein-Knowles, P.; Henriksen, A.
Structure of the mitochondrial beta-ketoacyl-[acyl carrier protein] synthase from Arabidopsis and its role in fatty acid synthesis
FEBS Lett.
577
170-174
2004
Arabidopsis thaliana (Q8L3X9), Arabidopsis thaliana
Yasuno, R.; von Wettstein-Knowles, P.; Wada, H.
Identification and molecular characterization of the beta-ketoacyl-[acyl carrier protein] synthase component of the Arabidopsis mitochondrial fatty acid synthase
J. Biol. Chem.
279
8242-8251
2004
Arabidopsis thaliana (Q8L3X9), Arabidopsis thaliana
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