| Literature DB >> 7592335 |
E R van den Bergh1, T A van der Kooij, L Dijkhuizen, W G Meijer.
Abstract
Xanthobacter flavus employs two fructosebisphosphatase (FBPase)-sedoheptulosebisphosphatase (SBPase) enzymes. One of these is constitutively expressed and has a high FBPase-to-SBPase ratio. The alternative enzyme, which is encoded by cbbF, is induced during autotrophic growth. The cbbF gene was expressed in Escherichia coli, and the FBPase was purified to homogeneity. The purified enzyme has a specific FBPase activity of 114 mumol/min/mg of protein, a Michaelis constant for fructosebisphosphate of 3 microM, and a low FBPase-to-SBPase ratio. CbbF was activated by ATP and inhibited by Ca2+.Entities:
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Year: 1995 PMID: 7592335 PMCID: PMC177410 DOI: 10.1128/jb.177.20.5860-5864.1995
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490