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Enzyme Nomenclature
Information on EC 2.3.1.271 - L-glutamate-5-semialdehyde N-acetyltransferase
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EC Tree
2.3.1.271 L-glutamate-5-semialdehyde N-acetyltransferaseIUBMB Comments
The enzyme, characterized from the yeast Saccharomyces cerevisiae Sigma1278b, N-acetylates L-glutamate-5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
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Word Map
- 2.3.1.271
- l-proline
-
l-azetidine-2-carboxylic
-
signalosome
- pombe
-
detoxifies
-
schizosaccharomyces
- sigma1278b
-
four-membered
-
misfolded
-
znii2cys6
-
fission
-
photomorphogenesis
-
binuclear
-
triplets
-
spacing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AZC acetyltransferase
AZC-detoxifying enzyme
L-azetidine-2-carboxylate N-acetyltransferase
MPR1
Mpr1p
MPR2
-
-
-
-
MPR1
-
-
-
-
MPR1
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-glutamate-5-semialdehyde = CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-glutamate-5-semialdehyde N-acetyltransferase
The enzyme, characterized from the yeast Saccharomyces cerevisiae Sigma1278b, N-acetylates L-glutamate-5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
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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
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
acetyl-CoA + L-DELTA1-pyrroline 5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + L-DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
acetyl-CoA + L-glutamate 5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
acetyl-CoA + 4-hydroxy-L-proline
CoA + N-acetyl-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + 4-hydroxy-L-proline
CoA + N-acetyl-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
Kloeckera africana
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-2-carboxylate
CoA + N-acetyl-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + azetidine-3-carboxylic acid
CoA + N-acetylazetidine-3-carboxylic acid
lowest activity
-
-
?
acetyl-CoA + azetidine-3-carboxylic acid
CoA + N-acetylazetidine-3-carboxylic acid
lowest activity
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + glutamate-gamma-semialdehyde
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + glutamate-gamma-semialdehyde
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylate
CoA + N-acetyl-L-azetidine-2-carboxylate
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
highest activity
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
Saccharomyces cerevisiae Sigma1278
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
highest activity
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
-
?
acetyl-CoA + L-DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
Saccharomyces cerevisiae Sigma1278
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
acetyl-CoA + L-DELTA1-pyrroline 5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + L-glutamate 5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + cis-4-hydroxy-L-proline
CoA + N-acetyl-cis-4-hydroxy-L-proline
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + DELTA1-pyrroline-5-carboxylate + H2O
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + glutamate-gamma-semialdehyde
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + glutamate-gamma-semialdehyde
CoA + N-acetyl-glutamate-gamma-semialdehyde
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-azetidine-2-carboxylic acid
CoA + N-acetyl-L-azetidine-2-carboxylic acid
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
Saccharomyces cerevisiae Sigma1278
-
-
-
-
?
acetyl-CoA + L-glutamate-5-semialdehyde
CoA + N-acetyl-L-glutamate 5-semialdehyde
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0049
acetyl-CoA
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
0.011
acetyl-CoA
mutant enzyme LK63R/L117V, at pH 8.5 and 30°C
0.013
acetyl-CoA
mutant enzyme F65L/L117V, at pH 8.5 and 30°C
0.7
azetidine-2-carboxylate
mutant enzyme F65L, at pH 8.5 and 30°C
1.2
azetidine-2-carboxylate
mutant enzyme K63R, at pH 8.5 and 30°C
1.2
azetidine-2-carboxylate
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
1.4
azetidine-2-carboxylate
mutant enzyme L117V, at pH 8.5 and 30°C
1.6
azetidine-2-carboxylate
wild type enzyme, at pH 8.5 and 30°C
1.6
azetidine-2-carboxylate
mutant enzyme K63P, at pH 8.5 and 30°C
1.7
azetidine-2-carboxylate
mutant enzyme LK63R/L117V, at pH 8.5 and 30°C
1.8
azetidine-2-carboxylate
mutant enzyme F65L/L117V, at pH 8.5 and 30°C
2.2
azetidine-2-carboxylate
mutant enzyme K63R/F65L, at pH 8.5 and 30°C
3.3
azetidine-2-carboxylate
mutant enzyme F65G, at pH 8.5 and 30°C
1.17
L-azetidine-2-carboxylic acid
mutant enzyme Y168A, at pH 8.5 and 30°C
1.5 - 2
L-azetidine-2-carboxylic acid
wild type enzyme, at pH 8.5 and 30°C
2.91
L-azetidine-2-carboxylic acid
mutant enzyme Y89A, at pH 8.5 and 30°C
3.49
L-azetidine-2-carboxylic acid
mutant enzyme Y157A, at pH 8.5 and 30°C
4.03
L-azetidine-2-carboxylic acid
mutant enzyme Y166F, at pH 8.5 and 30°C
12.7
L-azetidine-2-carboxylic acid
mutant enzyme Y121A, at pH 8.5 and 30°C
20.9
L-azetidine-2-carboxylic acid
-
wild type enzyme, at pH 7.5 and 30°C
60.9
L-azetidine-2-carboxylic acid
mutant enzyme R145A, at pH 8.5 and 30°C
64.4
L-azetidine-2-carboxylic acid
mutant enzyme R145G, at pH 8.5 and 30°C
78.4
L-azetidine-2-carboxylic acid
mutant enzyme R145W, at pH 8.5 and 30°C
92.7
L-azetidine-2-carboxylic acid
mutant enzyme Y75A, at pH 8.5 and 30°C
116
L-azetidine-2-carboxylic acid
mutant enzyme R145E, at pH 8.5 and 30°C
135.8
L-azetidine-2-carboxylic acid
-
mutant enzyme N178A, at pH 7.5 and 30°C
192
L-azetidine-2-carboxylic acid
mutant enzyme R145D, at pH 8.5 and 30°C
407
L-azetidine-2-carboxylic acid
-
mutant enzyme N135A, at pH 7.5 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.1
acetyl-CoA
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
3 - 6
azetidine-2-carboxylate
wild type enzyme, at pH 8.5 and 30°C
11
azetidine-2-carboxylate
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
16
azetidine-2-carboxylate
mutant enzyme F65G, at pH 8.5 and 30°C
19
azetidine-2-carboxylate
mutant enzyme K63P, at pH 8.5 and 30°C
31
azetidine-2-carboxylate
mutant enzyme F65L, at pH 8.5 and 30°C
31
azetidine-2-carboxylate
mutant enzyme K63R, at pH 8.5 and 30°C
38
azetidine-2-carboxylate
mutant enzyme F65L/L117V, at pH 8.5 and 30°C
46
azetidine-2-carboxylate
mutant enzyme LK63R/L117V, at pH 8.5 and 30°C
48
azetidine-2-carboxylate
mutant enzyme L117V, at pH 8.5 and 30°C
51
azetidine-2-carboxylate
mutant enzyme K63R/F65L, at pH 8.5 and 30°C
4.31
L-azetidine-2-carboxylic acid
mutant enzyme Y157A, at pH 8.5 and 30°C
7.09
L-azetidine-2-carboxylic acid
mutant enzyme R145D, at pH 8.5 and 30°C
7.2
L-azetidine-2-carboxylic acid
-
mutant enzyme N178A, at pH 7.5 and 30°C
12.8
L-azetidine-2-carboxylic acid
mutant enzyme Y121A, at pH 8.5 and 30°C
13.7
L-azetidine-2-carboxylic acid
mutant enzyme Y166F, at pH 8.5 and 30°C
19.3
L-azetidine-2-carboxylic acid
mutant enzyme Y168A, at pH 8.5 and 30°C
24.8
L-azetidine-2-carboxylic acid
mutant enzyme Y89A, at pH 8.5 and 30°C
33.5
L-azetidine-2-carboxylic acid
wild type enzyme, at pH 8.5 and 30°C
38.6
L-azetidine-2-carboxylic acid
-
mutant enzyme N135A, at pH 7.5 and 30°C
63.1
L-azetidine-2-carboxylic acid
mutant enzyme R145E, at pH 8.5 and 30°C
73.6
L-azetidine-2-carboxylic acid
mutant enzyme Y75A, at pH 8.5 and 30°C
225
L-azetidine-2-carboxylic acid
mutant enzyme R145W, at pH 8.5 and 30°C
287.2
L-azetidine-2-carboxylic acid
-
wild type enzyme, at pH 7.5 and 30°C
304
L-azetidine-2-carboxylic acid
mutant enzyme R145G, at pH 8.5 and 30°C
609
L-azetidine-2-carboxylic acid
mutant enzyme R145A, at pH 8.5 and 30°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
0.0022
acetyl-CoA
mutant enzyme K63R/F65L, at pH 8.5 and 30°C
0.0023
acetyl-CoA
mutant enzyme F65L/L117V, at pH 8.5 and 30°C
0.0023
acetyl-CoA
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
0.0037
acetyl-CoA
mutant enzyme LK63R/L117V, at pH 8.5 and 30°C
4.7
azetidine-2-carboxylate
mutant enzyme F65G, at pH 8.5 and 30°C
9.5
azetidine-2-carboxylate
mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C
12
azetidine-2-carboxylate
mutant enzyme K63P, at pH 8.5 and 30°C
21
azetidine-2-carboxylate
mutant enzyme F65L/L117V, at pH 8.5 and 30°C
22
azetidine-2-carboxylate
wild type enzyme, at pH 8.5 and 30°C
23
azetidine-2-carboxylate
mutant enzyme K63R/F65L, at pH 8.5 and 30°C
25
azetidine-2-carboxylate
mutant enzyme K63R, at pH 8.5 and 30°C
27
azetidine-2-carboxylate
mutant enzyme LK63R/L117V, at pH 8.5 and 30°C
33
azetidine-2-carboxylate
mutant enzyme L117V, at pH 8.5 and 30°C
46
azetidine-2-carboxylate
mutant enzyme F65L, at pH 8.5 and 30°C
0.0369
L-azetidine-2-carboxylic acid
mutant enzyme R145D, at pH 8.5 and 30°C
0.548
L-azetidine-2-carboxylic acid
mutant enzyme R145E, at pH 8.5 and 30°C
0.794
L-azetidine-2-carboxylic acid
mutant enzyme Y75A, at pH 8.5 and 30°C
1
L-azetidine-2-carboxylic acid
mutant enzyme Y121A, at pH 8.5 and 30°C
1.24
L-azetidine-2-carboxylic acid
mutant enzyme Y157A, at pH 8.5 and 30°C
2.88
L-azetidine-2-carboxylic acid
mutant enzyme R145W, at pH 8.5 and 30°C
3.41
L-azetidine-2-carboxylic acid
mutant enzyme Y166F, at pH 8.5 and 30°C
4.72
L-azetidine-2-carboxylic acid
mutant enzyme R145G, at pH 8.5 and 30°C
8.51
L-azetidine-2-carboxylic acid
mutant enzyme Y89A, at pH 8.5 and 30°C
10
L-azetidine-2-carboxylic acid
mutant enzyme R145A, at pH 8.5 and 30°C
16.5
L-azetidine-2-carboxylic acid
mutant enzyme Y168A, at pH 8.5 and 30°C
22.4
L-azetidine-2-carboxylic acid
wild type enzyme, at pH 8.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
L-azetidine-2-carboxylic acid
-
wild type enzyme, at pH 7.5 and 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
-
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
a null mutant of the MPR1 and MPR2 genes shows hypersensitivity to ethanol stress
malfunction
-
a null mutant of the MPR1 and MPR2 genes shows hypersensitivity to ethanol stress
-
metabolism
Mpr1 is an antioxidant enzyme that acetylates toxic DELTA1-pyrroline-5-carboxylate involved in reactive oxygen species generation
metabolism
the enzyme confers resistance to the proline analogue azetidine-2-carboxylate
metabolism
the enzyme converts DELTA1-pyrroline-5-carboxylate/glutamate-gamma-semialdehyde into N-acetyl-glutamate-gamma-semialdehyde for arginine synthesis in the mitochondria, indicating that the enzyme mediates the proline and arginine metabolic pathways. Enzyme-dependent arginine synthesis confers stress tolerance
metabolism
-
Mpr1 is an antioxidant enzyme that acetylates toxic DELTA1-pyrroline-5-carboxylate involved in reactive oxygen species generation
-
metabolism
-
the enzyme converts DELTA1-pyrroline-5-carboxylate/glutamate-gamma-semialdehyde into N-acetyl-glutamate-gamma-semialdehyde for arginine synthesis in the mitochondria, indicating that the enzyme mediates the proline and arginine metabolic pathways. Enzyme-dependent arginine synthesis confers stress tolerance
-
metabolism
-
the enzyme confers resistance to the proline analogue azetidine-2-carboxylate
-
physiological function
the enzyme protects yeast cells from DELTA1-pyrroline-5-carboxylate-induced oxidative stress by reducing reactive oxygen species
physiological function
the enzyme protects yeast cells from freezing stress by reducing the intracellular levels of reactive oxygen species
physiological function
-
the enzyme protects yeast cells from H2O2, heat shock, and ethanol stress by reducing intracellular reactive oxygen species levels. The enzyme is required for resistance to l-azetidine-2-carboxylic acid
physiological function
-
the enzyme protects yeast cells from H2O2, heat shock, and ethanol stress by reducing intracellular reactive oxygen species levels. The enzyme is required for resistance to l-azetidine-2-carboxylic acid
-
physiological function
-
the enzyme protects yeast cells from freezing stress by reducing the intracellular levels of reactive oxygen species
-
physiological function
-
the enzyme protects yeast cells from DELTA1-pyrroline-5-carboxylate-induced oxidative stress by reducing reactive oxygen species
-
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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). MPR1_YEASX
229
0
26233
Swiss-Prot
other Location (Reliability: 2)
ACA1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
209
0
23809
Swiss-Prot
other Location (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with the substrate cis-4-hydroxy-L-proline, sitting drop vapor diffusion method, using 100 mM Bistris-HCl (pH 5.5), 240 mM MgCl2, and 20.5% (w/v) PEG 3350
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F65G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F65L
F65L/L117V
F65L/N203K
the mutant shows lower activity compared to the wild type enzyme
F65L/N203R
the mutant shows lower activity compared to the wild type enzyme
K63P
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K63R
the mutant shows higher azetidine-2-carboxylate resistance compared to the wild type
K63R/F65L
the mutant shows higher catalytic efficiency compared to the wild type enzyme
K63R/F65L/L117V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L117V
the mutant shows higher catalytic efficiency compared to the wild type enzyme
LK63R/L117V
the mutant shows higher catalytic efficiency compared to the wild type enzyme
N135A
-
the mutation causes a remarkable increase in the apparent Km value for acetyl-CoA
N178A
-
the mutation causes a large reduction in the apparent kcat value for acetyl-CoA
N203K
the mutant exhibits higher activity and 2.4fold longer activity half-live at 50°C than the wild type enzyme
N203R
the mutant with about wild type activity exhibits 2.2fold longer activity half-live at 50°C than the wild type enzyme
R145A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
R145D
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
R145E
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
R145G
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
R145W
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
Y121A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
Y157A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
Y166F
Y168A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
Y75A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
Y89A
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
Y989A
the mutation results in a 2.6fold reduction in the kcat/Km ratio for l-azetidine-2-carboxylic acid compared to the wild type enzyme
F65L
-
the mutant shows higher catalytic efficiency compared to the wild type enzyme
-
F65L/L117V
K63R
-
the mutant shows higher azetidine-2-carboxylate resistance compared to the wild type
-
L117V
-
the mutant shows higher catalytic efficiency compared to the wild type enzyme
-
N135A
-
the mutation causes a remarkable increase in the apparent Km value for acetyl-CoA
-
N178A
-
the mutation causes a large reduction in the apparent kcat value for acetyl-CoA
-
R145W
-
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
-
Y166F
Y168A
-
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
-
F65L
the mutant exhibits slightly lower activity compared to the wild type enzyme
F65L
the mutant shows higher catalytic efficiency compared to the wild type enzyme
F65L/L117V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F65L/L117V
the mutant shows higher azetidine-2-carboxylate resistance compared to the wild type
Y166F
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
Y166F
the mutation leads to a remarkable decrease of the kcat/Km value for l-azetidine-2-carboxylic acid compared to the wild type enzyme
F65L/L117V
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
F65L/L117V
-
the mutant shows higher azetidine-2-carboxylate resistance compared to the wild type
-
Y166F
-
the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
-
Y166F
-
the mutation leads to a remarkable decrease of the kcat/Km value for l-azetidine-2-carboxylic acid compared to the wild type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography and DEAE Toyopearl 650M column chromatography
-
Ni-Sepharose 6 column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Xanthi
expressed in Zygosaccharomyces rouxii strains ATCC 2623 and ATCC 42981
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hibi, T.; Yamamoto, H.; Nakamura, G.; Takagi, H.
Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
65
169-172
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma1278
brenda
Du, X.; Takagi, H.
N-acetyltransferase Mpr1 confers ethanol tolerance on Saccharomyces cerevisiae by reducing reactive oxygen species
Appl. Microbiol. Biotechnol.
75
1343-1351
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma1278b
brenda
Wada, M.; Okabe, K.; Kataoka, M.; Shimizu, S.; Yokota, A.; Takagi, H.
Distribution of L-azetidine-2-carboxylate N-acetyltransferase in yeast
Biosci. Biotechnol. Biochem.
72
582-586
2008
Pichia kudriavzevii, Meyerozyma guilliermondii, Candida maltosa, Candida parapsilosis, Wickerhamomyces anomalus, Kluyveromyces lactis, no activity in Candida boidinii, no activity in Saccharomyces cerevisiae, no activity in Candida tropicalis, no activity in Cryptococcus albidus, no activity in Rhodotorula glutinis, Komagataella pastoris, Ogataea pini, Cystobasidium minutum, Sporidiobolus salmonicolor, Lachancea thermotolerans, Ogataea methanolica, Wickerhamia fluorescens, Kloeckera africana, no activity in Candida nitratophila, no activity in Candida sonorensis, no activity in Pichia angusta, no activity in Pichia capsulata, no activity in Pichia finlandica, no activity in Pichia naganishii, no activity in Cryptococcus laurentii, no activity in Cryptococcus terreus, no activity in Rhodotorula aurantiaca, no activity in Rhodotorula mucilaginosa, no activity in Sporidiobolus salmonicolor, no activity in Sporobolomyces salmonicolor, [Candida] saitoana, Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae, no activity in Saccharomyces cerevisiae S288C, Saccharomyces cerevisiae Sigma1278b (E9P8D2), Saccharomyces cerevisiae Sigma1278b
brenda
Iinoya, K.; Kotani, T.; Sasano, Y.; Takagi, H.
Engineering of the yeast antioxidant enzyme Mpr1 for enhanced activity and stability
Biotechnol. Bioeng.
103
341-352
2009
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Nishimura, A.; Nasuno, R.; Takagi, H.
The proline metabolism intermediate DELTA1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast
FEBS Lett.
586
2411-2416
2012
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma 1278b (E9P8D2)
brenda
Nishimura, A.; Kotani, T.; Sasano, Y.; Takagi, H.
An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1 Oxidative stress-induced arginine synthesis and its physiological role
FEMS Yeast Res.
10
687-698
2010
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Kotani, T.; Takagi, H.
Identification of amino acid residues essential for the yeast N-acetyltransferase Mpr1 activity by site-directed mutagenesis
FEMS Yeast Res.
8
607-614
2008
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Pribylova, L.; Sychrova, H.
Expression of the Saccharomyces cerevisiae MPR1 gene encoding N-acetyltransferase in Zygosaccharomyces rouxii confers resistance to L-azetidine-2-carboxylate
Folia Microbiol. (Praha)
51
203-207
2006
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Nomura, M.; Nakamori, S.; Takagi, H.
Characterization of novel acetyltransferases found in budding and fission yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid
J. Biochem.
133
67-74
2003
Schizosaccharomyces pombe
brenda
Du, X.; Takagi, H.
N-acetyltransferase Mpr1 confers freeze tolerance on Saccharomyces cerevisiae by reducing reactive oxygen species
J. Biochem.
138
391-397
2005
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Nasuno, R.; Hirase, S.; Norifune, S.; Watanabe, D.; Takagi, H.
Structure-based molecular design for thermostabilization of N-acetyltransferase Mpr1 involved in a novel pathway of L-arginine synthesis in yeast
J. Biochem.
159
271-277
2015
Saccharomyces cerevisiae (E9P8D2)
brenda
Shichiri, M.; Hoshikawa, C.; Nakamori, S.; Takagi, H.
A novel acetyltransferase found in Saccharomyces cerevisiae Sigma1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid
J. Biol. Chem.
276
41998-42002
2001
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma1278b (E9P8D2), Saccharomyces cerevisiae Sigma1278b
brenda
Mai Hoa, B.; Hibi, T.; Nasuno, R.; Matsuo, G.; Sasano, Y.; Takagi, H.
Production of N-acetyl cis-4-hydroxy-l-proline by the yeast N-acetyltransferase Mpr1
J. Biosci. Bioeng.
114
160-165
2012
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Tsai, F.; Zhang, X.; Ulanov, A.; Widholm, J.
The application of the yeast N-acetyltransferase MPR1 gene and the proline analogue L-azetidine-2-carboxylic acid as a selectable marker system for plant transformation
J. Exp. Bot.
61
2561-2573
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma 1278b
brenda
Zhang, X.; Takagi, H.; Widholm, J.
Expression of a novel yeast gene that detoxifies the proline analog azetidine-2-carboxylate confers resistance during tobacco seed germination, callus and shoot formation
Plant Cell Rep.
22
615-622
2004
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Nomura, M.; Takagi, H.
Role of the yeast, acetyltransferase Mpr1 in oxidative stress Regulation of oxygen reactive species caused by a toxic proline catabolism intermediate
Proc. Natl. Acad. Sci. USA
101
12616-12621
2004
Saccharomyces cerevisiae (E9P8D2), Saccharomyces cerevisiae Sigma1278b (E9P8D2)
brenda
Nasuno, R.; Hirano, Y.; Itoh, T.; Hakoshima, T.; Hibi, T.; Takagi, H.
Structural and functional analysis of the yeast n-Acetyltransferase mpr1 involved in oxidative stress tolerance via proline metabolism
Proc. Natl. Acad. Sci. USA
110
11821-11826
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae Sigma1278b
brenda
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