The Purloined Letter: bacterial orthologs of archaeal NMN adenylyltransferase are domains within multifunctional transcription regulator NadR.
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چکیده
منابع مشابه
Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica.
The three activities of NadR were demonstrated in purified protein and assigned to separate domains by missense mutations. The N-terminal domain represses transcription of genes for NAD synthesis and salvage. The C-terminal domain has nicotinamide ribose kinase (NmR-K; EC 2.7.1.22) activity, which is essential for assimilation of NmR, converting it internally to nicotinamide mononucleotide (NMN...
متن کاملRibosylnicotinamide kinase domain of NadR protein: identification and implications in NAD biosynthesis.
NAD is an indispensable redox cofactor in all organisms. Most of the genes required for NAD biosynthesis in various species are known. Ribosylnicotinamide kinase (RNK) was among the few unknown (missing) genes involved with NAD salvage and recycling pathways. Using a comparative genome analysis involving reconstruction of NAD metabolism from genomic data, we predicted and experimentally verifie...
متن کاملThe Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity.
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 functi...
متن کاملBifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism.
Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase and an ADP-ribose (ADPR) pyrophosphatase domain. While most members of this enzyme family, such as that from a model cyanobacterium Synechocystis sp., are involved primarily in nicotinamide adenine dinucleotide (NAD) salvage/recycling pathways, its close homolog in a category-A biode...
متن کاملNew Insights into the Phylogeny and Molecular Classification of Nicotinamide Mononucleotide Deamidases
Nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle (PNC). It catalyzes the conversion of NMN to nicotinic acid mononucleotide, which is later converted to NAD(+) by entering the Preiss-Handler pathway. However, very few biochemical data are available regarding this enzyme. This paper represents the first complete molecular characteri...
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ورودعنوان ژورنال:
- Journal of molecular microbiology and biotechnology
دوره 1 1 شماره
صفحات -
تاریخ انتشار 1999