3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics.

@article{Kato19783HexulosephosphateSF,
  title={3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics.},
  author={Nobuo Kato and Hiroshi Ohashi and Yoshiki Tani and Kazuhiro Ogata},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={523 1},
  pages={236-44}
}
3-Hexulosephosphate synthase (D-arabino-3-hexulose 6-phosphate formaldehyde lyase) was purified from an obligate methylotroph, Methylomonas aminofaciens, to homogeneity as judged by polyacrylamide gel electrophoresis and analytical ultracentrifugation. The molecular weight was determined to be 45 000-47 000 by sedimentation velocity and gel filtration. The enzyme appears to be composed of two identical subunits (Mr = 23 000). A bivalent cation is required for the activation and stabilization of… CONTINUE READING

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