Information on EC 2.3.1.105 - alkylglycerophosphate 2-O-acetyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.3.1.105
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RECOMMENDED NAME
GeneOntology No.
alkylglycerophosphate 2-O-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate = CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ether lipid metabolism
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-
Metabolic pathways
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-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase
Involved in the biosynthesis of thrombocyte activating factor in animal tissues.
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CAS REGISTRY NUMBER
COMMENTARY hide
76773-96-1
not distinguishable from EC 2.3.1.67 in Chemical Abstracts
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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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
acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate
CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate
CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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29% decline in subcellular fraction P3A activity, 43% decline in subcellular fraction P3B activity and 7% decline in subcellular fraction P3D activity
Alkaline phosphatase
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92-95% activity lost for subcellular fractions P3A and P3B
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ATP
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little effect on the enzyme activity for the subcellular fraction P3A, 55-64% decline in the subcellular fraction P3B
CaCl2
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1 mM CaCl2 inhibits 73% and 24% activity of subcellular fractions P3B and P3D respectively
dithiothreitol
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EDTA
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inhibits 30% fraction P3D, does not inhibit subcellular fraction P3A
MgADP-
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inhibitory effects less severe than MgATP
MgAMP
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less inhibitory effect than MgADP
MgATP2-
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extreme inhibition in all microsomal fractions
MgCl2
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at 2 mM: 30, 28 and 58% inhibition of subcellular fractions P3A, P3B and P3D activities respectively
Sodium vanadate
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inhibits at concentrations above 0.025 mM
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-alkyl-sn-glycero-3-phosphocholine
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small increase of activity
EDTA
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47.8% activity in absence of both EDTA and mercaptoethanol
mercaptoethanol
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47.8% activity in absence of both EDTA and mercaptoethanol
additional information
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activity increases in 2.4fold by preincubation with ATP, MgCl2 and high speed supernatant fractions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.226
acetyl-CoA
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
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subcellular fractions R and P3
8.4 - 9
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subcellular fractions P
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cortex and medulla
Manually annotated by BRENDA team
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highest activity
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isolation of four subcellular fractions: S, R and P3 from cerebral cortices and P from nerve cell bodies
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isolation of three subcellular fractions: P3A, P3B and P3D, using NaF, EDTA and mercaptoethanol to preserve the activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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TCA-precipitation method for the determination of 1-alkyl-sn-glycero-3-phosphate:acetyl-CoA acetyltransferase in human renal tissue
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.105)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)