2.3.1.271: L-glutamate-5-semialdehyde N-acetyltransferase
This is an abbreviated version!
For detailed information about L-glutamate-5-semialdehyde N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.271
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2.3.1.271
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l-proline
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l-azetidine-2-carboxylic
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signalosome
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pombe
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detoxifies
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schizosaccharomyces
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sigma1278b
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four-membered
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misfolded
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znii2cys6
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fission
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photomorphogenesis
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binuclear
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triplets
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spacing
- 2.3.1.271
- l-proline
-
l-azetidine-2-carboxylic
-
signalosome
- pombe
-
detoxifies
-
schizosaccharomyces
- sigma1278b
-
four-membered
-
misfolded
-
znii2cys6
-
fission
-
photomorphogenesis
-
binuclear
-
triplets
-
spacing
Reaction
Synonyms
AZC acetyltransferase, AZC-detoxifying enzyme, L-azetidine-2-carboxylate N-acetyltransferase, MPR1, Mpr1p, MPR2, ppr1(+), Ppr1p
ECTree
2.3.1.271 L-glutamate-5-semialdehyde N-acetyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.271 - L-glutamate-5-semialdehyde N-acetyltransferase
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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
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the mutation causes a remarkable increase in the apparent Km value for acetyl-CoA
N178A
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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
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the mutant shows higher catalytic efficiency compared to the wild type enzyme
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F65L/L117V
K63R
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the mutant shows higher azetidine-2-carboxylate resistance compared to the wild type
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L117V
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the mutant shows higher catalytic efficiency compared to the wild type enzyme
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N135A
-
the mutation causes a remarkable increase in the apparent Km value for acetyl-CoA
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N178A
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the mutation causes a large reduction in the apparent kcat value for acetyl-CoA
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R145W
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the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and acetyl-CoA
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Y166F
Y168A
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the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
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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
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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
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Y166F
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the mutation causes a large reduction in the affinity for l-azetidine-2-carboxylic acid and increases affinity for acetyl-CoA
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Y166F
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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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