[113] Nicotinamide phosphoribosyltransferase and NAD pyrophosphorylase from Lactobacillus fructosus

Ohtsu, Eiji; Nishizuka, Yasutomi

doi:10.1016/s0076-6879(71)18070-6

Cited by 11 publications

(4 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…that lack both the de novo pathway and the Preiss-Handler route (Preiss and Handler, 1958), the direct synthesis of the pyridine dinucleotide can only proceed through NMN utilization. In such microorganisms, the enzyme NMN adenylyltransferase has been found to be specific for NMN, unable to react with NaMN (Ohtsu and Nishizuka, 1971;Kasarov and Moat, 1973). It is noteworthy that NMN adenylyltransferase is the only enzyme in NAD+ biosynthetic pathway to be located in the cell nucleus (Hogeboom and Schneider, 1952).…”

Section: B N M N Adenylyltransferasementioning

confidence: 99%

“…For example, in Haemophilus haemoglobinophilus and Lactobacillusfructosus, ATP is absolutely required for the NamPRTase activity (Kasarov and Moat, 1973;Ohtsu and Nishizuka, 1971). In rat liver, ATP was found to stimulate the activity by lowering the K,,, value for nicotinamide from 0.1 M to 1 pkf (Powanda et al, 1969;Dietrich, 1971;Dietrich and Muniz, 1972).…”

Section: Nicotinamide Phosphoribosyltransferasementioning

confidence: 99%

See 1 more Smart Citation

Enzymology of Nad ⁺ Synthesis

Magni

Amici

Emanuelli

et al. 1999

Advances in Enzymology - And Related Areas of Molecular Biology

193

194

View full text Add to dashboard Cite

Section: B N M N Adenylyltransferasementioning

confidence: 99%

Section: Nicotinamide Phosphoribosyltransferasementioning

confidence: 99%

Enzymology of Nad ⁺ Synthesis

Magni

Amici

Emanuelli

et al. 1999

Advances in Enzymology - And Related Areas of Molecular Biology

193

194

View full text Add to dashboard Cite

“…However it remains one of the few genes involved in the NAD ϩ biosynthetic pathway not to have been cloned and sequenced from any organism. The enzyme has been identified and characterized in its catalytic properties from several prokaryotic sources (6,10,26). It has been purified to homogeneity and extensively characterized by us from yeast, bull testis, and human placenta (4,12,24), but its instability and relatively low concentration in cell extracts precluded obtaining enzyme preparations suitable for gene isolation.…”

Section: Nadmentioning

confidence: 99%

Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea

et al. 1997

View full text Add to dashboard Cite

The enzyme nicotinamide mononucleotide (NMN) adenylyltransferase (EC 2.7.7.1) catalyzes the synthesis of NAD ؉ and nicotinic acid adenine dinucleotide. It has been purified to homogeneity from cellular extracts of the thermophilic archaeon Sulfolobus solfataricus. Through a database search, a highly significant match was found between its N-terminal sequence and a hypothetical protein coded by the thermophilic archaeon Methanococcus jannaschii MJ0541 open reading frame (GenBank accession no. U67503). The MJ0541 gene was isolated, cloned into a T7-based vector, and expressed in Escherichia coli cells, yielding a high level of thermophilic NMN adenylyltransferase activity. The expressed protein was purified to homogeneity by a single-step chromatographic procedure. Both the subunit molecular mass and the N-terminal sequence of the pure recombinant protein were as expected from the deduced amino acid sequence of the MJ0541 open reading frame-encoded protein. Molecular and kinetic properties of the enzymes from both archaea are reported and compared with those already known for the mesophilic eukaryotic NMN adenylyltransferase. NADϩ synthesis can be accomplished either via de novo pathways or through preformed pyridine ring salvage routes (13). All such pathways converge to the reaction nicotinamide mononucleotide (NMN) (or nicotinic acid mononucleotide) ϩ ATP 7 NAD ϩ (or nicotinic acid adenine dinucleotide) ϩ PP i , which is catalyzed by the enzyme NMN adenylyltransferase (EC 2.7.7.1). Interestingly, this is the only enzyme in the biosynthetic pathway to be located in the cell nucleus (15). Numerous examples of a fluctuation of NMN adenylyltransferase activity during the DNA synthesis phase of the cell cycle have been reported (14,23,32). More recently, it has been proposed that the nuclear localization of the enzyme could be related to the consistent demand for NAD ϩ as a substrate for nuclear poly(ADP) ribosylation reactions (29, 34), thus suggesting a major role for the enzyme in cellular metabolism. In prokaryotes, the NMN adenylyltransferase gene, designated nadD, was mapped and demonstrated to be essential for viability (16). However it remains one of the few genes involved in the NAD ϩ biosynthetic pathway not to have been cloned and sequenced from any organism. The enzyme has been identified and characterized in its catalytic properties from several prokaryotic sources (6,10,26). It has been purified to homogeneity and extensively characterized by us from yeast, bull testis, and human placenta (4, 12, 24), but its instability and relatively low concentration in cell extracts precluded obtaining enzyme preparations suitable for gene isolation. We have previously reported the presence of NMN adenylyltransferase in the thermophilic archaeon Sulfolobus solfataricus (28). Purification to homogeneity of the S. solfataricus enzyme and determination of its N-terminal sequence allowed us to recognize the MJ0541 open reading frame (ORF) from the Methanococcus jannaschii genome sequence as the NMN adenylyltransferase ...

show abstract

“…["PIHAP 2 fraction was prepared and subjected to density gradient centrifugation as described in Fig.2. Fractions corresponding to (A) the top (1 -6), (B) middle (7)(8)(9)(10)(11)(12) and (C) bottom (13)(14)(15)(16)(17)(18)(19)(20) and (B) bottom ( 1 -1) were calculated to give an estimate of the radioactivity incorporated into proteinbound and free poly(ADP-Rib) respectively. The arrows indicate the time at which nicotinamide (50 mM) was added and the subsequent decrease in acid-insoluble radioactivity at the top (0---) and bottom (&a) of the gradients was determined associated with both protein-bound and free poly-(ADP-Rib).…”

Section: Synthesis Of Free Poly(adp-rib)mentioning

confidence: 99%

The Modification of Nuclear Proteins by ADP‐ribosylation

Rickwood

MacGillivray

Whish

1977

European Journal of Biochemistry

View full text Add to dashboard Cite

When incubated in vitro purified mouse nuclei incorporate NAD into poly(ADP-Rib). Analysis of the product on CsCl/urea gradients showed that a large proportion of the poly(ADP-Rib) was not attached to protein. The free poly(ADP-Rib) did not appear to arise through degradation and its chain length was significantly longer than the poly(ADP-Rib) attached to proteins. Fractionation of the proteins on hydroxyapatite revealed that tissue-specific modification of both the histones and non-histone proteins, had occurred. In the case of one protein species there was evidence for the existence of several forms with different numbers of ADP-Rib residues.It is now more than ten years since the synthesis of poly(ADP-Rib) in isolated nuclei was first demonstrated; it was shown that when nuclei were incubated in vitro with labelled NAD the radioactivity was incorporated exclusively into poly(ADP-Rib) [l]. More recently evidence has been presented to show that this polymer is also synthesized in vivo [2]. Poly(ADP-Rib) is a polynucleotide-like molecule but, in contrast to the other polynucleotides of the cell, its functional role in the cell remains unclear. It has been reported that poly(ADP-Rib) is attached to the nuclear proteins (for a review see [3]) and as such it could modify the characteristics of the proteins to which it is bound, in the same way as phosphorylation and acetylation can also modify the interaction of histones with DNA. Two problems emerge from the evidence presently available. The first concerns which proteins of the nucleus act as acceptors for the poly(ADP-Rib) molecules. So far only the histones have been identified with certainty as being modified by the polymer [4-61, but with the improved techniques now available (see [7]) it is possible to examine the role of most of the nuclear proteins in this process. The second problem relates to the large number of conflicting reports as to the rate of synthesis of poly(ADP-Rib) at different times of the cell cycle [8] and the difficulty of correlating polymer production and its modification of nuclear proteins with particular events in the cell cycle or with changes in gene activity. For some years these laboratories have been involved in developing procedures for the preparation and analysis of nuclear proteins (see [7,9,10]) and in this paper we describe the application of some of our techniques to study the modification of nuclear proteins by poly-(ADP-Rib) in a number of mouse cells.

show abstract

[113] Nicotinamide phosphoribosyltransferase and NAD pyrophosphorylase from Lactobacillus fructosus

Cited by 11 publications

References 4 publications

Enzymology of Nad ⁺ Synthesis

Enzymology of Nad ⁺ Synthesis

Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea

The Modification of Nuclear Proteins by ADP‐ribosylation

Contact Info

Product

Resources

About

[113] Nicotinamide phosphoribosyltransferase and NAD pyrophosphorylase from Lactobacillus fructosus

Cited by 11 publications

References 4 publications

Enzymology of Nad + Synthesis

Enzymology of Nad + Synthesis

Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea

The Modification of Nuclear Proteins by ADP‐ribosylation

Contact Info

Product

Resources

About

Enzymology of Nad ⁺ Synthesis

Enzymology of Nad ⁺ Synthesis