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Information on EC 2.3.1.40 - acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase and Organism(s) Escherichia coli and UniProt Accession P31119

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This record set is specific for:
Escherichia coli
UNIPROT: P31119 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acyl-acyl carrier protein (acyl-acp) synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl-acyl carrier protein (acyl-ACP) synthase
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-
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acyltransferase, acyl-[acyl carrier protein]-phospholipid
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = an [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
show the reaction diagram
bifunctional protein exhibits both 2-acylglycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synhtase activities in vitro
an acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = an [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
show the reaction diagram
bifunctional protein exhibits both 2-acylglycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synhtase activities in vitro
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O-acyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37257-18-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-(acyl-carrier protein) + O-(2-acyl-sn-glycero-3-phospho) ethanolamine
(acyl-carrier protein) + O-(1,2-diacyl-sn-glycero-3-phospho) ethanolamine
show the reaction diagram
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specific for C1-position of glycerol-phosphate backbone, the acyl-component of the acyl-(acyl-carrier-protein) may be 3-hydroxydecanoate, 3-hydroxylaurate, 3-hydroxymyristate and 3-hydroxyoctanoate (tentatively identified)
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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activation, 0.2 M
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no stimulation by coenzyme A, ATP, GTP, UTP, glucosamine 1-phosphate, UDP-N-acetylglucosamine, Triton X-100, lipid A, alkaline treated lipid A or alkaline treated lipid A annealed with Escherichia coli phospholipids
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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about half-maximal activity at pH 5.0, about 60% of maximal activity at pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K 12 derivates LCH 25, 26, 28, 55, 56
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H36A
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mutant lacks 2-acylglycerophosphoethanolamine acyltransferase activity, whereas it retains acyl-acyl carrier protein synthase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
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inactivation after 2-5 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, solubilization by sonic disruption
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, S.S.; Heath, E.C.
The incorporation of beta-hydroxy fatty acids into a phospholipid of Escherichia coli B
J. Biol. Chem.
244
6605-6616
1969
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Jackowski, S.; Jackson, P.D.; Rock, C.O.
Sequence and function of the aas gene in Escherichia coli
J. Biol. Chem.
269
2921-2928
1994
Escherichia coli (P31119), Escherichia coli
Manually annotated by BRENDA team
Heath, R.J.; Rock, C.O.
A conserved histidine is essential for glycerolipid acyltransferase catalysis
J. Bacteriol.
180
1425-1430
1998
Escherichia coli
Manually annotated by BRENDA team