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4.31
-
mutant enzyme Y157A, at pH 8.5 and 30°C
7.09
-
mutant enzyme R145D, at pH 8.5 and 30°C
7.2
-
mutant enzyme N178A, at pH 7.5 and 30°C
12.8
-
mutant enzyme Y121A, at pH 8.5 and 30°C
13.57
-
at pH 8.5 and 30°C
13.7
-
mutant enzyme Y166F, at pH 8.5 and 30°C
17.9
-
at pH 8.5 and 30°C
19.3
-
mutant enzyme Y168A, at pH 8.5 and 30°C
24.8
-
mutant enzyme Y89A, at pH 8.5 and 30°C
33.5
-
wild type enzyme, at pH 8.5 and 30°C
38.6
-
mutant enzyme N135A, at pH 7.5 and 30°C
63.1
-
mutant enzyme R145E, at pH 8.5 and 30°C
73.6
-
mutant enzyme Y75A, at pH 8.5 and 30°C
225
-
mutant enzyme R145W, at pH 8.5 and 30°C
287.2
-
wild type enzyme, at pH 7.5 and 30°C
304
-
mutant enzyme R145G, at pH 8.5 and 30°C
609
-
mutant enzyme R145A, at pH 8.5 and 30°C
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1.17
-
mutant enzyme Y168A, at pH 8.5 and 30°C
1.5
2
wild type enzyme, at pH 8.5 and 30°C
1.62
-
at pH 8.5 and 30°C
2.91
-
mutant enzyme Y89A, at pH 8.5 and 30°C
3.49
-
mutant enzyme Y157A, at pH 8.5 and 30°C
4.03
-
mutant enzyme Y166F, at pH 8.5 and 30°C
12.7
-
mutant enzyme Y121A, at pH 8.5 and 30°C
20.9
-
wild type enzyme, at pH 7.5 and 30°C
60.9
-
mutant enzyme R145A, at pH 8.5 and 30°C
64.4
-
mutant enzyme R145G, at pH 8.5 and 30°C
78.4
-
mutant enzyme R145W, at pH 8.5 and 30°C
92.7
-
mutant enzyme Y75A, at pH 8.5 and 30°C
116
-
mutant enzyme R145E, at pH 8.5 and 30°C
135.8
-
mutant enzyme N178A, at pH 7.5 and 30°C
192
-
mutant enzyme R145D, at pH 8.5 and 30°C
407
-
mutant enzyme N135A, at pH 7.5 and 30°C
1.43
-
ATP-diphosphate exchange
2
-
ATP-diphosphate exchange
5.3
-
ATP-diphosphate exchange
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-
Substrate discrimination by prolyl-tRNA synthetase from various higher plants
1972
Norris, R.D.; Fowden, L.
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11
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Biosynthesis of proline in Pseudomonas aeruginosa. Properties of gamma-glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase
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Substrate selectivities of proline hydroxylases
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Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution
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Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae
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The proline metabolism intermediate DELTA1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast
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An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1 Oxidative stress-induced arginine synthesis and its physiological role
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Identification of amino acid residues essential for the yeast N-acetyltransferase Mpr1 activity by site-directed mutagenesis
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Expression of the Saccharomyces cerevisiae MPR1 gene encoding N-acetyltransferase in Zygosaccharomyces rouxii confers resistance to L-azetidine-2-carboxylate
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Characterization of novel acetyltransferases found in budding and fission yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid
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N-acetyltransferase Mpr1 confers freeze tolerance on Saccharomyces cerevisiae by reducing reactive oxygen species
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Structure-based molecular design for thermostabilization of N-acetyltransferase Mpr1 involved in a novel pathway of L-arginine synthesis in yeast
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A novel acetyltransferase found in Saccharomyces cerevisiae Sigma1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid
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Production of N-acetyl cis-4-hydroxy-l-proline by the yeast N-acetyltransferase Mpr1
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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
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Expression of a novel yeast gene that detoxifies the proline analog azetidine-2-carboxylate confers resistance during tobacco seed germination, callus and shoot formation
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Role of the yeast, acetyltransferase Mpr1 in oxidative stress Regulation of oxygen reactive species caused by a toxic proline catabolism intermediate
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Proc. Natl. Acad. Sci. USA
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Structural and functional analysis of the yeast n-Acetyltransferase mpr1 involved in oxidative stress tolerance via proline metabolism
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Proc. Natl. Acad. Sci. USA
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Characterisation of a putative glutamate 5-kinase from Leishmania donovani
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Bacterial sarcosine oxidase identification of novel substrates and a biradical reaction intermediate
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