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PMID: 10464228 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity.

Journal of bacteriology ·Vol. 181 ·No. 17 ·1999-09-00 ·Pages 5509-11

Raffaelli N, Lorenzi T, Mariani PL, Emanuelli M, Amici A, Ruggieri S, Magni G

Abstract

The first identification and characterization of a catalytic activity associated with NadR protein is reported. A computer-aided search for sequence similarity revealed the presence in NadR of a 29-residue region highly conserved among known nicotinamide mononucleotide adenylyltransferases. The Escherichia coli nadR gene was cloned into a T7-based vector and overexpressed. In addition to functionally specific DNA binding properties, the homogeneous recombinant protein catalyzes NAD synthesis from nicotinamide mononucleotide and ATP.

MeSH Terms
Amino Acid Sequence Bacterial Proteins Cloning, Molecular DNA/metabolism Escherichia coli Gene Expression Molecular Sequence Data Nicotinamide-Nucleotide Adenylyltransferase/metabolism Recombinant Fusion Proteins/genetics,isolation & purification,metabolism Repressor Proteins/genetics,isolation & purification,metabolism
Chemicals
Bacterial Proteins NadR protein, bacteria Recombinant Fusion Proteins Repressor Proteins DNA Nicotinamide-Nucleotide Adenylyltransferase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Raffaelli N
Istituto di Biochimica, Facoltà di Medicina, Università di Ancona, 60131 Ancona, Italy.
Lorenzi T
Mariani P L
Emanuelli M
Amici A
Ruggieri S
Magni G
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.181.17.5509-5511.1999
Published
1999-09-00
Pages
5509-11
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC94063
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.181.17.5509-5511.1999 PMC Full Text View journal details
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