Takenaka, Shinji et al. published their research in Applied and Environmental Microbiology in 2014 |CAS: 32462-30-9

The Article related to acetyltransferase chryseobacterium aminosalicylate protein sequence phenylglycine phylogeny, Enzymes: Separation-Purification-General Characterization and other aspects.Reference of H-Phg(4-OH)-OH

On March 31, 2014, Takenaka, Shinji; Yoshida, Kenji; Tanaka, Kosei; Yoshida, Ken-ichi published an article.Reference of H-Phg(4-OH)-OH The title of the article was Molecular characterization of a novel N-acetyltransferase from Chryseobacterium sp.. And the article contained the following:

N-Acetyltransferase from Chryseobacterium sp. strain 5-3B is an acetyl CoA (acetyl-CoA)-dependent enzyme that catalyzes the enantioselective transfer of an acetyl group from acetyl-CoA to the amino group of L-2-phenylglycine to produce (2S)-2-acetylamino-2-phenylacetic acid. We purified the enzyme from strain 5-3 B and deduced the N-terminal amino acid sequence. The gene, designated natA, was cloned with two other hypothetical protein genes; the three genes probably form a 2.5-kb operon. The deduced amino acid sequence of NatA showed high levels of identity to sequences of putative N-acetyltransferases of Chryseobacterium spp. but not to other known arylamine and arylalkylamine N-acetyltransferases. Phylogenetic anal. indicated that NatA forms a distinct lineage from known N-acetyltransferases. We heterologously expressed recombinant NatA (rNatA) in Escherichia coli and purified it. RNatA showed high activity for L-2-phenylglycine and its chloro- and hydroxyl-derivatives The Km and Vmax values for L-2-phenylglycine were 0.145 ± 0.026 mM and 43.6 ± 2.39 μmol·min-1·mg protein-1, resp. The enzyme showed low activity for 5-aminosalicylic acid and 5-hydroxytryptamine, which are reported as good substrates of a known arylamine N-acetyltransferase and an arylalkylamine N-acetyltransferase. RNatA had a comparatively broad acyl donor specificity, transferring acyl groups to L-2-phenylglycine and producing the corresponding 2-acetylamino-2-phenylacetic acids (relative activity with acetyl donors acetyl-CoA, propanoyl-CoA, butanoyl-CoA, pentanoyl-CoA, and hexanoyl-CoA, 100:108:122:10:<1). The experimental process involved the reaction of H-Phg(4-OH)-OH(cas: 32462-30-9).Reference of H-Phg(4-OH)-OH

The Article related to acetyltransferase chryseobacterium aminosalicylate protein sequence phenylglycine phylogeny, Enzymes: Separation-Purification-General Characterization and other aspects.Reference of H-Phg(4-OH)-OH

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