Pyruvate carboxylase from Rhizobium etli: mutant characterization, nucleotide sequence, and physiological role
نویسندگان
چکیده
منابع مشابه
Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli.
The effects of mutations in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase have been determined for the forward reaction to form oxaloacetate, the reverse reaction to form MgATP, the oxamate-induced decarboxylation of oxaloacetate, the phosphorylation of MgADP by carbamoyl phosphate, and the bicarbonate-dependent ATPase reaction. Additional studies wit...
متن کاملNucleotide sequence of the Rhizobium etli nodS gene.
The complete nucleotide sequence of the nodS gene from the bean-nodulating Rhizobium etli, presumably encoding a methyltransferase, was determined. A phylogenetic analysis of five different NodS proteins from three genera of Gram- soil bacteria, Azorhizobium, Bradyrhizobium and Rhizobium, was performed.
متن کاملMechanisms of Inhibition of Rhizobium etli Pyruvate Carboxylase by l-Aspartate
L-aspartate is a regulatory feedback inhibitor of the biotin-dependent enzyme pyruvate carboxylase in response to increased levels of tricarboxylic acid cycle intermediates. Detailed studies of L-aspartate inhibition of pyruvate carboxylase have been mainly confined to eukaryotic microbial enzymes, and aspects of its mode of action remain unclear. Here we examine its inhibition of the bacterial...
متن کاملPhysiological role of pyruvate carboxylase in a thermophilic bacillus.
A prototrophic, thermophilic bacillus is in a state of biotin insufficiency when grown in medium consisting of inorganic salts and a carbon source. The effect of this biotin deficiency on the growth rate is severe only if the functioning of pyruvate carboxylase is essential for the utilization of the particular growth substrate. A mutant, PC2, of the thermophile devoid of active pyruvate carbox...
متن کاملRhizobium etli asparaginase II
Bacterial L-asparaginase has been a universal component of therapies for childhood acute lymphoblastic leukemia since the 1970s. Two principal enzymes derived from Escherichia coli and Erwinia chrysanthemi are the only options clinically approved to date. We recently reported a study of recombinant L-asparaginase (AnsA) from Rhizobium etli and described an increasing type of AnsA family members...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1996
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.178.20.5960-5970.1996