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A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis

The Journal of Biological Chemistry

Jul 23, 2004

Silvia GaravagliaMenico Rizzi

Abstract

NAD kinase catalyzes the magnesium-dependent phosphorylation of NAD, representing the sole source of freshly synthesized NADP in all organisms. The enzyme is essential for the growth of the deadly multidrug-resistant pathogen Mycobacterium tuberculosis and is an attractive target for no...read more

Mentioned in this Paper

Magnesium Measurement
Carboxy-Terminal Amino Acid
Allosteric Site
NAD+ kinase
Pathogenic Organism
Tertiary Protein Structure
Protein Phosphorylation
Protein Structure, Quaternary
Crystallography, X-Ray
Protein Conformation
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A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis

The Journal of Biological Chemistry

Jul 23, 2004

Silvia GaravagliaMenico Rizzi

PMID: 15269221

DOI: 10.1074/jbc.m406586200

Abstract

NAD kinase catalyzes the magnesium-dependent phosphorylation of NAD, representing the sole source of freshly synthesized NADP in all organisms. The enzyme is essential for the growth of the deadly multidrug-resistant pathogen Mycobacterium tuberculosis and is an attractive target for no...read more

Mentioned in this Paper

Magnesium Measurement
Carboxy-Terminal Amino Acid
Allosteric Site
NAD+ kinase
Pathogenic Organism
Tertiary Protein Structure
Protein Phosphorylation
Protein Structure, Quaternary
Crystallography, X-Ray
Protein Conformation

Similar Papers Found In These Feeds

Phosphorylation

Phosphorylation is the attachment of a phosphoryl group, which is often provided by ATP, to a protein by a specific type of enzyme called kinase. Discover the latest research on phosphorylation here.

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

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Paper Details
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  • References
  • Citations23
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
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