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Information on EC 2.3.1.331 - phenylglycine N-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.331
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.331 phenylglycine N-acetyltransferase
IUBMB Comments
The enzyme has been isolated from the bacterium Chryseobacterium sp. 5-3B. Reduced activity has been observed with L-2-phenylglycine methyl ester, L-2-chlorophenylglycine and L-4-hydroxyphenylglycine.
The expected taxonomic range for this enzyme is: unclassified Chryseobacterium
showSynonyms
NatA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NatA
NatA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-phenylglycine = (2S)-2-acetylamino-2-phenylacetic acid + CoA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-phenylgylcine N-acetyltransferase
The enzyme has been isolated from the bacterium Chryseobacterium sp. 5-3B. Reduced activity has been observed with L-2-phenylglycine methyl ester, L-2-chlorophenylglycine and L-4-hydroxyphenylglycine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + (+/-)-1-phenylethylamine
?
-
Substrates: 6.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + (+/-)-1-phenylethylamine
CoA + ?
Substrates: 6.3% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + 2-chlorophenylglycine
?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 4-aminobenzoic acid
?
-
Substrates: 2.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + 4-chlorophenylglycine
?
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 5-aminosalicylic acid
?
-
Substrates: 5.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + D-4-hydroxy-2-phenylglycine
?
-
Substrates: 2.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-2-(2-chlorophenyl)glycine
?
-
Substrates: 57% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-2-chlorophenylglycine
CoA + ?
Substrates: 56.9% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
-
Substrates: 98% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-2-phenylglycine
CoA + ?
Substrates: 98% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-4-(2-chlorophenyl)glycine
?
-
Substrates: 7.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-4-chlorophenylglycine
CoA + ?
Substrates: 7.4% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-homophenylalanine
?
-
Substrates: 2.0% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + DL-phenylalanine
?
-
Substrates: 1.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-2-chlorophenylglycine
CoA + N-acetyl-L-2-chlorophenylglycine
Substrates: 52.9% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
CoA + (2S)-2-acetylamino-2-phenylacetic acid
Substrates: 100% activity
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine methyl ester
?
Substrates: 59% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine methyl ester
CoA + N-acetyl-L-2-phenylglycine methyl ester
Substrates: 75.5% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-4-hydroxy-2-phenylglycine
?
-
Substrates: 17% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-4-hydroxyphenylglycine
?
Substrates: very weak activity
Products: -
Products: -
?
acetyl-CoA + L-4-hydroxyphenylglycine
CoA + N-acetyl-L-4-hydroxyphenylglycine
Substrates: 16.7% activity compared to L-2-phenylglycine
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
Substrates: 100% activity
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
-
Substrates: 100% activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows low activity for 5-aminosalicylic acid (5.5%), 4-aminobenzoic acid (2.5%), D-4-hydroxyphenylglycine (2.4%), DL-homophenylalanine (1.9%), DL-phenylalanine (1.5%), and 5-hydroxytryptamine and D-2-phenylglycine (less than 1%, respectively)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-2-phenylglycine
Products: -
Products: -
-
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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 + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + L-2-phenylglycine
(2S)-2-acetylamino-2-phenylacetic acid + CoA
-
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
35.2% residual activity after 1 h at 1 mM
additional information
Mn2+, EDTA, tiron, alpha,alpha'-dipyridyl, phenylglyoxal, phenylmethylsulfonyl fluoride, iodoacetic acid and iodoacetamide do not markedly inhibit the enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
L-2-phenylglycine
mutant enzyme S85A, at pH 7.5 and 30°C
0.111
L-2-phenylglycine
wild type enzyme, at pH 7.5 and 30°C
0.19
L-2-phenylglycine
mutant enzyme Y40F, at pH 7.5 and 30°C
0.5 - 2
L-2-phenylglycine
mutant enzyme Y40A, at pH 7.5 and 30°C
0.76
L-2-phenylglycine
mutant enzyme T122A, at pH 7.5 and 30°C
0.99
L-2-phenylglycine
mutant enzyme W28A, at pH 7.5 and 30°C
1.1
L-2-phenylglycine
mutant enzyme I29A, at pH 7.5 and 30°C
1.9
L-2-phenylglycine
mutant enzyme N25A, at pH 7.5 and 30°C
4.6
L-2-phenylglycine
mutant enzyme M35A, at pH 7.5 and 30°C
12.9
L-2-phenylglycine
mutant enzyme F33A, at pH 7.5 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.21
L-2-phenylglycine
mutant enzyme I29A, at pH 7.5 and 30°C
1.3
L-2-phenylglycine
mutant enzyme T122A, at pH 7.5 and 30°C
1.9
L-2-phenylglycine
mutant enzyme W28A, at pH 7.5 and 30°C
2.4
L-2-phenylglycine
mutant enzyme N25A, at pH 7.5 and 30°C
3.9
L-2-phenylglycine
mutant enzyme S85A, at pH 7.5 and 30°C
6.9
L-2-phenylglycine
mutant enzyme Y40F, at pH 7.5 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
L-2-phenylglycine
mutant enzyme I29A, at pH 7.5 and 30°C
0.75
L-2-phenylglycine
mutant enzyme F33A, at pH 7.5 and 30°C
1.3
L-2-phenylglycine
mutant enzyme N25A, at pH 7.5 and 30°C
1.7
L-2-phenylglycine
mutant enzyme T122A, at pH 7.5 and 30°C
1.9
L-2-phenylglycine
mutant enzyme W28A, at pH 7.5 and 30°C
8.4
L-2-phenylglycine
mutant enzyme M35A, at pH 7.5 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9
-
highly active at pH 8.0-9.0 for the biotransformation of 2-phenylglycine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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.
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). W0SLW8_9FLAO
161
0
18090
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E83Q
the mutant shows 28% activity with L-2-phenylcglycine compared to the wild type enzyme
E83Q/Y133F
the mutant shows 1.0% activity with L-2-phenylcglycine compared to the wild type enzyme
F33A
the mutant shows 1.3% activity with L-2-phenylcglycine compared to the wild type enzyme
I29A
the mutant shows 0.32% activity with L-2-phenylcglycine compared to the wild type enzyme
K131A
the mutant shows 71% activity with acetyl-CoA compared to the wild type enzyme
K135A
the mutant shows 105% activity with acetyl-CoA compared to the wild type enzyme
L126A
the mutant shows 84% activity with acetyl-CoA compared to the wild type enzyme
L132A
the mutant shows 87% activity with acetyl-CoA compared to the wild type enzyme
M35A
the mutant shows 14% activity with L-2-phenylcglycine compared to the wild type enzyme
M87A
the mutant shows 25% activity with acetyl-CoA compared to the wild type enzyme
N25A
the mutant shows 2.2% activity with L-2-phenylcglycine compared to the wild type enzyme
Q94A
the mutant shows 104% activity with acetyl-CoA compared to the wild type enzyme
S85A
the mutant shows 110% activity with L-2-phenylcglycine compared to the wild type enzyme
T122A
the mutant shows 3.0% activity with L-2-phenylcglycine compared to the wild type enzyme
V89A
the mutant shows 27% activity with acetyl-CoA compared to the wild type enzyme
W28A
the mutant shows 3.2% activity with L-2-phenylcglycine compared to the wild type enzyme
Y100F
the mutant shows 56% activity with acetyl-CoA compared to the wild type enzyme
Y133F
the mutant shows 3.1% activity with L-2-phenylcglycine and 28% activity with acetyl-CoA compared to the wild type enzyme
Y40A
the mutant shows 48% activity with L-2-phenylcglycine compared to the wild type enzyme
Y40F
the mutant shows 61% activity with L-2-phenylcglycine compared to the wild type enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, in 20 mMTris/HCl buffer (pH8.0), 1 month, the enzyme remains stable
-
4°C, 50 mM sodium potassium phosphate buffer (pH 7.5) containing 0.3 M NaCl, more than 1 month, no loss of activity
4°C, storage medium, more than 1 month, less than 20% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl-Toyopearl column chromatography, and Cosmogel His-accept column chromatography
streptomycin sulfate precipitation, ammonium sulfate precipitation, butyl cellulofine chromatography, and DEAE-cellulofine chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takenaka, S.; Yoshida, K.; Tanaka, K.; Yoshida, K.
Molecular characterization of a novel N-acetyltransferase from Chryseobacterium sp.
Appl. Environ. Microbiol.
80
1770-1776
2014
Chryseobacterium sp. (W0SLW8)
brenda
Takenaka, S.; Honma, Y.; Yoshida, K.; Yoshida, K.
Enantioselective N-acetylation of 2-phenylglycine by an unusual N-acetyltransferase from Chryseobacterium sp.
Biotechnol. Lett.
35
1053-1059
2013
Chryseobacterium sp. 5-3B
brenda
Takenaka, S.; Ozeki, T.; Tanaka, K.; Yoshida, K.I.
Homology modeling and prediction of the amino acid residues participating in the transfer of acetyl-CoA to arylalkylamine by the N-acetyltransferase from Chryseobacterium sp.
Biotechnol. Lett.
39
1699-1707
2017
Chryseobacterium sp. 5-3B (W0SLW8)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.331)
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