Single and twinned crystals of ribulose-1,5-bisphosphate carboxylase-oxygenase from Alcaligenes eutrophus.
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چکیده
منابع مشابه
Ribulose-bisphosphate carboxylase manipulation in the hydrogen bacterium Alcaligenes eutrophus.
separated by an intervening stretch of DNA, variable in length depending on the particular species of origin (Curtis & Hazelkorn, 1983; Shinozaki & Sugiura, 1983). The gene from S,.rzc~c.lioc.oc~r~us PCC30 1 (Reichelt & Delaney, 1983) has been cloned into the ampr region of PLa2311 (Remaut ct al., 1981) with expression controlled by the strong temperature-sensitive leftward promoter (PI ) of ba...
متن کاملStructure of ribulose-1,5-bisphosphate carboxylase-oxygenase: Form III crystals.
A new crystal form (III) of tobacco leaf ribulosebisphosphate carboxylase [3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39] has been grown by dialysis procedures, and is suitable for structural studies at near atomic resolution. The crystals exhibit birefringence, grow as pseudo-regular rhombic dodecahedrons, and belong to the tetragonal space group P4(2)2(1)2 with a = b = 149 A, ...
متن کاملRibulose 1,5-bisphosphate carboxylase/oxygenase from Pseudomonas oxalacticus.
Ribulose 1,5-bisphosphate carboxylase/oxygenase was purified by a rapid, facile procedure from formate-grown Pseudomonas oxalaticus. The electrophoretically homogeneous enzyme had specific activities of 1.9 mumol of CO2 fixed per min per mg of protein and 0.15 mumol of O2 consumed per min per mg of protein. The amino acid composition was similar to that of other bacterial sources of the enzyme....
متن کاملRibulose-1,5-bisphosphate carboxylase/oxygenase activase cDNAs from Nicotiana tabacum.
Rubisco-the key regulatory enzyme in photosynthetic carbon assimilation-is activated in vivo by the chloroplast enzyme Rubisco activase (Portis, 1990). Previous studies in which Rubisco antisense DNA mutants of tobacco were used have revealed that under some circumstances Rubisco activase can play a central role in regulating the photosynthetic process (Rodermel et al., 1988; Quick et al., 1991...
متن کاملRibulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents the in vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase.
The rate of CO(2) fixation by ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) following addition of ribulose 1,5-bisphosphate (RuBP) to fully activated enzyme, declined with first-order kinetics, resulting in 50% loss of rubisco activity after 10 to 12 minutes. This in vitro decline in rubisco activity, termed fall-over, was prevented if purified rubisco activase protein and ATP were ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85147-5