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Literature DB >> 7730286

Nucleoside diphosphate kinase from Escherichia coli.

N Almaula¹, Q Lu, J Delgado, S Belkin, M Inouye.

Abstract

Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine residues, including Ser-119 and Ser-121, appear to be phosphorylated. A Ser119Ala/Ser121Ala double mutant (i.e., with a Ser-to-Ala double mutation at positions 119 and 121), as well as Ser119Ala and Ser121Ala mutants, was isolated. All of these retained NDP kinase activity; also, both the Ser119Ala and Ser121Ala mutants could still be autophosphorylated. In the case of the double mutant, a slight autophosphorylation activity, which was resistant to acid treatment, was still detected, indicating that an additional minor autophosphorylation site besides His-117 exists. These results are discussed in light of the recent report of N. J. MacDonald et al. on the autophosphorylation of human NDP kinase (J. Biol. Chem. 268:25780-25789, 1993).

Entities: Chemical Gene Mutation Species

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Year: 1995 PMID： 7730286 PMCID： PMC176913 DOI： 10.1128/jb.177.9.2524-2529.1995

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

29 in total

1. NUCLEOSIDE TRIPHOSPHATE-NUCLEOSIDE DIPHOSPHATE TRANSPHOSPHORYLASE (NUCLEOSIDE DIPHOSPHOKINASE). I. ISOLATION OF THE CRYSTALLINE ENZYME FROM BREWERS' YEAST.

Authors: R L RATLIFF; R H WEAVER; H A LARDY; S A KUBY
Journal: J Biol Chem Date: 1964-01 Impact factor: 5.157

10. Two forms of the nucleoside diphosphate kinase of Pseudomonas aeruginosa 8830: altered specificity of nucleoside triphosphate synthesis by the cell membrane-associated form of the truncated enzyme.

Authors: S Shankar; S Kamath; A M Chakrabarty
Journal: J Bacteriol Date: 1996-04 Impact factor: 3.490

Nucleoside diphosphate kinase from Escherichia coli.

1. NUCLEOSIDE TRIPHOSPHATE-NUCLEOSIDE DIPHOSPHATE TRANSPHOSPHORYLASE (NUCLEOSIDE DIPHOSPHOKINASE). I. ISOLATION OF THE CRYSTALLINE ENZYME FROM BREWERS' YEAST.

2. Response of nucleoside diphosphate kinase to the adenylate energy charge.

3. Gas-phase hydrolysis of proteins and peptides.

4. Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate.

5. Evidence for a novel gene associated with low tumor metastatic potential.

6. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers.

7. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors.

8. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes.

9. Studies on transformation of Escherichia coli with plasmids.

10. Cold-sensitive mutant of Salmonella typhimurium defective in nucleosidediphosphokinase.

Review 1. Quaternary structure of nucleoside diphosphate kinases.

2. SwoHp, a nucleoside diphosphate kinase, is essential in Aspergillus nidulans.

3. Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism.

4. Genetic requirements for sensitivity of bacteriophage t7 to dideoxythymidine.

5. The nucleoside diphosphate kinase from mimivirus: a peculiar affinity for deoxypyrimidine nucleotides.

Review 6. Protein Ser/Thr/Tyr phosphorylation in the Archaea.

7. Elimination and utilization of oxidized guanine nucleotides in the synthesis of RNA and its precursors.

8. A modular minimal cell model: purine and pyrimidine transport and metabolism.

9. Escherichia coli nucleoside diphosphate kinase does not act as a uracil-processing DNA repair nuclease.

10. Two forms of the nucleoside diphosphate kinase of Pseudomonas aeruginosa 8830: altered specificity of nucleoside triphosphate synthesis by the cell membrane-associated form of the truncated enzyme.