A thermostable shikimate 5-dehydrogenase from the archaeon Archaeoglobus fulgidus
In: FEMS Microbiology Letters, Jg. 238 (2004-09-01), Heft 1, S. 101-106
Online
academicJournal
Zugriff:
Shikimate 5-dehydrogenase (SKDH; EC 1.1.1.25) catalyzes the reversible reduction of 3-dehydroshikimate to shikimate and is a key enzyme in the aromatic amino acid biosynthesis pathway. The shikimate 5-dehydrogenase gene, aroE, from Archaeoglobus fulgidus was cloned and overexpressed in Escherichia coli. The recombinant enzyme purified as a homodimer and yielded a maximum specific activity of 732 U/mg at 87 °C (with NADP+ as coenzyme). Apparent Km values for shikimate, NADP+, and NAD+ were estimated at 0.17±0.03 mM, 0.19±0.01 mM, and 11.4±0.4 mM, respectively. The half-life of the A. fulgidus SKDH is 2 h at the assay temperature (87 °C) and 17 days at 60 °C. Addition of 1 M NaCl or KCl stabilized the enzyme’s half-life to ∼70 h at 87 °C and ∼50 days at 60 °C. This work presents the first kinetic analysis of an archaeal SKDH. [Copyright &y& Elsevier]
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A thermostable shikimate 5-dehydrogenase from the archaeon Archaeoglobus fulgidus
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Autor/in / Beteiligte Person: | Lim, Sierin ; Schröder, Imke ; Monbouquette, Harold G. |
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Zeitschrift: | FEMS Microbiology Letters, Jg. 238 (2004-09-01), Heft 1, S. 101-106 |
Veröffentlichung: | 2004 |
Medientyp: | academicJournal |
ISSN: | 0378-1097 (print) |
DOI: | 10.1016/j.femsle.2004.07.023 |
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