Carboxylterminal deletion mutants of ribulosebisphosphate carboxylase from Rhodospirillum rubrum

FEBS Letters

Kane, Heather J.¹  Morell, Matthew K.¹  Andrews, T.John¹ 

[1] Research School of Biological Sciences, Australian National University, P.O. Box 475, Canberra, A.C.T. 2601, Australia

关键词: Ribulose bisphosphate carboxylase/oxygenase;    Rubisco;    Photosynthesis;    Site-directed mutagenesis;    Rhodospirillum rubrum;    ribulose-P2;    D-ribulose-1;    5-bisphosphate;    carboxyarabinitol-P2;    2'-carboxy-D-arabinitol-1;    5-bisphosphate;    carboxypentitol-P2;    unresolved isomeric mixture of carboxyarabinitol-P2 and 2'-carboxy-D-ribitol-1;    5-bisphosphate;    Epps;    N-2-hydroxyethylpiperazine-N'-3-propanesulfonic acid;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(90)80879-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The carboxylterminal octapeptide of ribulosebisphosphate carboxylase from Rhodospirillum rubrum, which lacks small subunits, shows homology to a highly conserved region near the amino terminus of the small subunits of hexadecameric ribulosebisphosphate carboxylases, which are composed of large and small subunits. Truncations of the R. rubrum enzyme, which partially or completely deleted the region of homology, demonstrated that the region is not an important determinant of the catalytic efficiency of the enzyme. A further truncation, which replaced the carboxylterminal 19 amino acid residues with a single terminal leucyl residue, yielded a Rubisco whose substrate-saturated catalytic rate resembled that of the wild-type enzyme but which had weaker affinities for ribulose-P₂ and CO₂.

【 授权许可】

Unknown