Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
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چکیده
منابع مشابه
Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with differing substrate specificities.
The carboxylated, 6-carbon reaction intermediate (3-keto-2-carboxyarabinitol 1,5-bisphosphate) from the ribulose-1,5-bisphosphate carboxylase reaction was obtained by denaturing the enzyme with acid during steady-state turnover. Carbon-13 NMR analysis indicates that this beta-keto acid exists in solution predominantly as the C-3 ketone (as opposed to the hydrate) form. In neutral solution the i...
متن کاملCrystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
The three-dimensional structure of the complex of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum, CO2, Mg2+, and ribulose bisphosphate has been determined with x-ray crystallographic methods to 2.6-A resolution. Ribulose-1,5-bisphosphate binds across the active site with the two phosphate groups in the two phosphate binding sites of the beta/alpha barrel. The oxygen atoms of t...
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Using results announced by Stevo Todorcevic we establish that if it is consistent that there is a supercompact cardinal then it is consistent that every locally compact perfectly normal space is paracompact. Modulo the large cardinal, this answers a question of S. Watson. We also solve a problem raised by the second author, proving that it is consistent with ZFC that every first countable hered...
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Partially purified ribulose-1,5-bisphosphate carboxylase (EC 4.1.1.39) was isolated from diploid and tetraploid cultivars of ryegrass (Lolium perenne L.) using two separate methods. The apparent K(m) (CO(2)) values for the enzymes prepared by either method did not differ significantly between diploid and tetraploid when assayed by two separate techniques. The unpurified enzymes from freshly lys...
متن کاملCatalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.
During catalysis, all Rubisco (D-ribulose-1,5-bisphosphate carboxylase/oxygenase) enzymes produce traces of several by-products. Some of these by-products are released slowly from the active site of Rubisco from higher plants, thus progressively inhibiting turnover. Prompted by observations that Form I Rubisco enzymes from cyanobacteria and red algae, and the Form II Rubisco enzyme from bacteri...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2006
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0600605103