Dissection of Escherichia coli glutamate 5-kinase: functional impact of the deletion of the PUA domain (Q46842175)

25 December 2017

title

Dissection of Escherichia coli glutamate 5-kinase: functional impact of the deletion of the PUA domain (English)

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25 December 2017

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2

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author name string

Isabel Pérez-Arellano

series ordinal

1

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25 December 2017

Javier Cervera

series ordinal

3

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language of work or name

English

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publication date

1 December 2005

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25 December 2017

published in

FEBS Letters

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25 December 2017

volume

579

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page(s)

6903-6908

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issue

30

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Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase

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Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition

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Glutamate-5-kinase from Escherichia coli: gene cloning, overexpression, purification and crystallization of the recombinant enzyme and preliminary X-ray studies

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The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function.

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The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic

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The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides [...]

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The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis

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Mechanism of oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study

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Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase.

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Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase

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Identifiers

DOI

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25 December 2017

PubMed ID

16337196

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25 December 2017