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0.35
-
mutant D189N, pH and temperature not specified in the publication
3.6
-
pH 7.5, 37°C, mutant enzyme C265S
7.83
-
pH 7.4, 30°C, mutant D125S sDAPL
12.45
-
pH 7.5, 37°C, mutant enzyme C291S
26
-
pH 7.4, 30°C, mutant D194S sDAPL
44.58
-
wild-type, pH and temperature not specified in the publication
53.7
-
pH 7.5, 37°C, wild-type enzyme
375.8
-
pH 7.4, 30°C, sDAPL
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0.03
-
pH 7.5, 37°C, mutant enzyme C291S
0.05
-
wild-type, pH and temperature not specified in the publication
0.13
-
pH 7.5, 37°C, mutant enzyme C265S
0.17
-
pH 7.5, 37°C, wild-type enzyme
0.282
-
pH 7.4, 30°C, sDAPL
0.293
-
pH 7.4, 30°C, mutant D194S sDAPL
0.346
-
pH 7.4, 30°C, mutant D125S sDAPL
12.9
-
mutant D189N, pH and temperature not specified in the publication
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Arginine racemase of Pseudomonas graveolens. I. Purification, crystallization, and properties
1971
Yorifuji, T.; Ogata, K.
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Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide
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A specific enzymatic procedure for the determination of neurotoxic components (derivatives of L-alpha,beta-diaminopropionic acid) in Lathyrus sativus
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Functional analysis of the genes encoding diaminopropionate ammonia lyase in Escherichia coli and Salmonella enterica serovar Typhimurium
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Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis
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Bisht, S.; Rajaram, V.; Bharath, S.R.; Kalyani, J.N.; Khan, F.; Rao, A.N.; Savithri, H.S.; Murthy, M.R.
J. Biol. Chem.
287
20369-20381
Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features
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Deka, G.; Bisht, S.; Savithri, H.S.; Murthy, M.R.N.
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118-128
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