Catalytic properties of enzymes from Erwinia carotovora involved in transamination of phenylpyruvate View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-03

AUTHORS

A. M. Paloyan, L. A. Stepanyan, S. A. Dadayan, A. A. Hambardzumyan, Gh. P. Halebyan, A. S. Saghiyan

ABSTRACT

Km for L-phenylalanine, L-glutamic acid, L-aspartic acid, and the corresponding keto acids were calculated, as well as Vmax was measured for the following pairs of substrates: L-phenylalanine-2-ketoglutarate, L-phenylalanine-oxaloacetate, L-glutamic acid-phenylpyruvate, and L-aspartic acid-phenylpyruvate for aminotransferases PAT1, PAT2, and PAT3 from Erwinia carotovora catalyzing transamination of phenylpyruvate. The ping-pong bi-bi mechanism was shown for the studied aminotransferases. The substrate inhibition (Ks) of PAT3 with 2-ketoglutarate and oxaloacetate was 10.23 ± 3.20 and 3.73 ± 1.99 mM, respectively. It was shown that L-β-(N-benzylamino)alanine was a competitive inhibitor with respect to L-phenylalanine for PAT1 (Ki = 0.32 ± 0.07 mM, Km = 0.45 ± 0.1 mM, Vmax = 11. 6 ± 0.4 U/mg) at 25 mM concentration of 2-ketoglutarate in the reaction medium. L-β-(N-methylamino)alanine is a noncompetitive inhibitor with respect to L-phenylalanine for PAT3 (KI = 138.4 ± 95.4 mM, Km = 13.7 ±3.9 mM, Vmax = 18.6 ± 4.1 U/mg) at 2 mM concentration of 2-ketoglutarate in the reaction medium. L-stereo isomers of nonprotein analogues of aromatic amino acids were studied as substrates for PAT1, PAT2, and PAT3. L-β-(2-Br-phenyl)alanine, L-β-(4-Br-phenyl)alanine, L-β-(2-F-phenyl)alanine, and L-(2-F)tryptophan were good substrates for all three aminotransferases; L-α-methyl-β-(2-Br-phenyl)alanine and L-O-benzyltyrosine were substrates only for PAT3; L-β-(4-F-phenyl)alanine was a substrate for PAT1 and PAT3. Thus, these analogues of aromatic amino acids can be stereoselectively synthesized using the studied aminotransferases in the presence of the corresponding keto acids. More... »

PAGES

106-112

References to SciGraph publications

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URI

http://scigraph.springernature.com/pub.10.1134/s0003683813020129

DOI

http://dx.doi.org/10.1134/s0003683813020129

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042894751


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