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Enzymatic analysis of a thermostabilized mutant of an Escherichia coli hygromycin B phosphotransferase.

Bioscience, biotechnology, and biochemistry - 1 Sept 2008

Nakamura Akira, Takakura Yasuaki, Sugimoto Naohisa, Takaya Naoki, Shiraki Kentaro, Hoshino Takayuki

Abstract excerpt

An Escherichia coli hygromycin B phosphotransferase (HPH) and its thermostabilized mutant protein, HPH5, containing five amino acid substitutions, D20G, A118V, S225P, Q226L, and T246A (Nakamura et al., J. Biosci. Bioeng., 100, 158-163 (2005)), obtained by an in vivo directed evolution procedure in Thermus thermophilus, were produced and purified from E. coli recombinants, and enzymatic comparisons were performed....

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PMID: 18776672
DOI: 10.1271/bbb.80285

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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