| Literature DB >> 6732239 |
S C Gumber, M W Loewus, F A Loewus.
Abstract
myo-Inositol-1-phosphate synthase [EC 5.5.1.4; 1L-myo-inositol-1-phosphate lyase, (isomerizing)] from Pinus ponderosa pollen has been partially purified and characterized. It has a pH optimum between 7.25 and 7.75. The km for D-glucose 6-phosphate (NAD+ constant at 1 mM) is 0.33 mM. Inhibition by p-chloromercuribenzoate and N-ethylmaleimide, and partial protection against this inhibition by D-glucose 6-phosphate in the presence of NAD+, suggests that there is sulfhydryl group involvement at the substrate binding site.Entities:
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Year: 1984 PMID: 6732239 DOI: 10.1016/0003-9861(84)90400-4
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013