Any feedback?
No. of entries
Information on EC 2.3.1.280 - (aminoalkyl)phosphonate N-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.280
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.280 (aminoalkyl)phosphonate N-acetyltransferase
IUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli, is able to acetylate a range of (aminoalkyl)phosphonic acids. Requires a divalent metal ion for activity.
The enzyme appears in viruses and cellular organisms
showSynonyms
aminoalkylphosphonate n-acetyltransferase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phnO
phnO
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + (aminomethyl)phosphonate = CoA + (acetamidomethyl)phosphonate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
(aminomethyl)phosphonate degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:(aminomethyl)phosphonate N-acetyltransferase
The enzyme, characterized from the bacterium Escherichia coli, is able to acetylate a range of (aminoalkyl)phosphonic acids. Requires a divalent metal ion for activity.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + (S)-1-aminoethylphosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 1-aminobutyl phosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 1-aminopropyl phosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-aminoethanesulfinic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-aminoethanesulfonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-aminoethyl phosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 2-aminoethylphosphonate
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-aminopropyl phosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-aminopropylphosphonate
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 4-aminobutylphosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
malonyl-CoA + (S)-1-aminoethylphosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
propionyl-CoA + (S)-1-aminoethylphosphonic acid
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: -
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1-aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylphosphonate for utilization of the phosphorus-containing moiety
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: -
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: reaction proceeds via an ordered, sequential kinetic mechanism with acetyl-CoA binding first followed by aminoalkylphosphonate. Attack by the amine on the thioester of AcCoA generates the tetrahedral intermediate that collapses to generate the products
Products: -
Products: -
?
acetyl-CoA + (S)-1-aminoethylphosphonate
CoA + ?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + (S)-1-aminoethylphosphonate
CoA + ?
Substrates: the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1-aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylphosphonate for utilization of the phosphorus-containing moiety
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + (S)-1-aminoethylphosphonate
CoA + ?
Substrates: the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1-aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylphosphonate for utilization of the phosphorus-containing moiety
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1-aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylphosphonate for utilization of the phosphorus-containing moiety
Products: -
Products: -
?
acetyl-CoA + (aminomethyl)phosphonate
CoA + (acetamidomethyl)phosphonate
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the enzyme requires a divalent metal ion for activity. It exhibits a preference for Ni2+ followed by Mn2+ and very poor activity with Mg2+
Mn2+
the enzyme requires a divalent metal ion for activity. It exhibits a preference for Ni2+ followed by Mn2+ and very poor activity with Mg2+
Ni2+
the enzyme requires a divalent metal ion for activity. It exhibits a preference for Ni2+ followed by Mn2+ and very poor activity with Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
(aminomethyl)phosphonate
pH 7.5, 25°C
0.17
(S)-1-aminoethylphosphonic acid
pH 7.5, 25°C
12.5
1-aminobutyl phosphonic acid
pH 7.5, 25°C
4.1
1-aminopropyl phosphonic acid
pH 7.5, 25°C
16.4
2-aminoethanesulfinic acid
pH 7.5, 25°C
18.9
2-aminoethanesulfonic acid
pH 7.5, 25°C
1.8
2-aminoethyl phosphonic acid
pH 7.5, 25°C
4
3-aminopropyl phosphonic acid
pH 7.5, 25°C
13
4-aminobutylphosphonic acid
pH 7.5, 25°C
0.06
acetyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
0.05
malonyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
0.07
propionyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7
(aminomethyl)phosphonate
pH 7.5, 25°C
13.3
(S)-1-aminoethylphosphonic acid
pH 7.5, 25°C
1
1-aminobutyl phosphonic acid
pH 7.5, 25°C
7.4
1-aminopropyl phosphonic acid
pH 7.5, 25°C
20
2-aminoethanesulfinic acid
pH 7.5, 25°C
14.8
2-aminoethanesulfonic acid
pH 7.5, 25°C
9
2-aminoethyl phosphonic acid
pH 7.5, 25°C
5.4
3-aminopropyl phosphonic acid
pH 7.5, 25°C
0.5
4-aminobutylphosphonic acid
pH 7.5, 25°C
13.1
acetyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
0.4
malonyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
14.7
propionyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
410
(aminomethyl)phosphonate
pH 7.5, 25°C
780
(S)-1-aminoethylphosphonic acid
pH 7.5, 25°C
800
1-aminobutyl phosphonic acid
pH 7.5, 25°C
180
1-aminopropyl phosphonic acid
pH 7.5, 25°C
120
2-aminoethanesulfinic acid
pH 7.5, 25°C
780
2-aminoethanesulfonic acid
pH 7.5, 25°C
5
2-aminoethyl phosphonic acid
pH 7.5, 25°C
140
3-aminopropyl phosphonic acid
pH 7.5, 25°C
380
4-aminobutylphosphonic acid
pH 7.5, 25°C
220
acetyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
800
malonyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
210
propionyl-CoA
cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in strain HO2735 the lacIq-specified repressor served to repress transcription of genes harbored in the pUHE23-2 vector
SwissProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1-aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylphosphonate for utilization of the phosphorus-containing moiety
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). PHNO_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
154
0
17933
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16499
electrospray ionization-mass spectrometry
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3) star cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Errey, J.C.; Blanchard, J.S.
Functional annotation and kinetic characterization of PhnO from Salmonella enterica
Biochemistry
45
3033-3039
2006
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZKE6)
brenda
Hove-Jensen, B.; McSorley, F.R.; Zechel, D.L.
Catabolism and detoxification of 1-aminoalkylphosphonic acids N-acetylation by the phnO gene product
PLoS ONE
7
e46416
2012
Escherichia coli (P16691), Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.280)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
