Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase

Kawai, Shigeyuki; Mori, Shiro; Mukai, Takako; Matsukawa, Hirokazu; Matuo, Yuhsi; Murata, Kousaku

doi:10.1016/s1389-1723(01)80294-2

Cited by 20 publications

(10 citation statements)

References 17 publications

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“…In addition, NADP + has been widely utilized as a diagnostic reagent component in the enzymatic analysis of blood and urine, and it can be produced by ATP‐dependent NAD kinase (Matsushita et al, 1986). M. tuberculosis enzyme which can utilize NAD and cheaper phosphodonor poly(P) to produce NADP, might be a good alternative to produce more commercially competitive NADP (Kawai et al, 2001).…”

Section: Nad Kinasementioning

confidence: 99%

Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets

Wang

Xie

2010

Journal Cellular Physiology

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NAD(P) is an indispensable cofactor for all organisms and its biosynthetic pathways are proposed as promising novel antibiotics targets against pathogens such as Mycobacterium tuberculosis. Six NAD(P) biosynthetic pathways were reconstructed by comparative genomics: de novo pathway (Asp), de novo pathway (Try), NmR pathway I (RNK-dependent), NmR pathway II (RNK-independent), Niacin salvage, and Niacin recycling. Three enzymes pivotal to the key reactions of NAD(P) biosynthesis are shared by almost all organisms, that is, NMN/NaMN adenylyltransferase (NMN/NaMNAT), NAD synthetase (NADS), and NAD kinase (NADK). They might serve as ideal broad spectrum antibiotic targets. Studies in M. tuberculosis have in part tested such hypothesis. Three regulatory factors NadR, NiaR, and NrtR, which regulate NAD biosynthesis, have been identified. M. tuberculosis NAD(P) metabolism and regulation thereof, potential drug targets and drug development are summarized in this paper.

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Section: Nad Kinasementioning

confidence: 99%

Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets

Wang

Xie

2010

Journal Cellular Physiology

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“…To overcome these drawbacks, an attempt was made to use the poly(P)-dependent NAD kinase activity of overexpressed NAD kinase (Ppnk) from M. tuberculosis to produce NADP þ from NAD þ and poly(P). 50) Poly(P) is a polymer of inorganic orthophosphate residues linked through phosphoanhydride bonds that are energetically equivalent to those of ATP, and it can be obtained commercially in large quantities at extremely low cost. 14) We found that NADP þ (36 mM) was produced from 50 mM NAD þ and 50 mg/ml poly(P) (metaphosphate) after a 24-h reaction using recombinant Ppnk.…”

Section: Application Of Nad Kinase To Mass Production Of Nadpmentioning

confidence: 99%

“…Collectively, production using Ppnk and poly(P) instead of ATP was successfully established, and the usefulness of poly(P) in the mass production of NADP þ was demonstrated for the first time. 50) Nevertheless, despite its usefulness, at present we are unable to produce various phosphorylated compounds from poly(P) due to limitations in the availability of different poly(P)-utilizing enzymes, such as Ppnk. To overcome this, we plan to confer poly(P)-utilizing ability on various ATP-specific kinases through protein engineering, and to use engineered kinases and poly(P) in the mass production of various valuable phosphorylated compounds.…”

Section: Application Of Nad Kinase To Mass Production Of Nadpmentioning

confidence: 99%

Structure and Function of NAD Kinase and NADP Phosphatase: Key Enzymes That Regulate the Intracellular Balance of NAD(H) and NADP(H)

Kawai

Murata

2008

Bioscience, Biotechnology, and Biochemistry

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107

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þ and NADPH) are undoubtedly significant and distinct. Hence, regulation of the intracellular balance of NAD(H) and NADP(H) is important. The key enzymes involved in the regulation are NAD kinase and NADP phosphatase. In 2000, we first succeeded in identifying the gene for NAD kinase, thereby facilitating worldwide studies of this enzyme from various organisms, including eubacteria, archaea, yeast, plants, and humans. Molecular biological study has revealed the physiological function of this enzyme, that is to say, the significance of NADP(H), in some model organisms. Structural research has elucidated the tertiary structure of the enzyme, the details of substratebinding sites, and the catalytic mechanism. Research on NAD kinase also led to the discovery of archaeal NADP phosphatase. In this review, we summarize the physiological functions, applications, and structure of NAD kinase, and the way we discovered archaeal NADP phosphatase.

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“…Because poly(P) is a much less expensive phosphoryl donor than ATP or any other triphosphonucleotide, Poly(P)/NTP-NAD kinase should have potential application values. In fact, Poly(P)/NTP-NAD kinases from mesophiles have already been used for the industrial production of NADP(H) from NAD(H) to decrease the producing cost of this diagnostic reagent [26]. Since thermo-stable poly(P)-dependent NAD kinase is more useful for enzymatic NADP(H) production, the hyperthermophilic archaea NAD kinases would have a higher application potential [19].…”

Section: Substrate Specificitymentioning

confidence: 99%

Molecular properties, functions, and potential applications of NAD kinases

Shi¹,

Li²,

Li³

et al. 2009

ABBS

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Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase

Cited by 20 publications

References 17 publications

Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets

Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets

Structure and Function of NAD Kinase and NADP Phosphatase: Key Enzymes That Regulate the Intracellular Balance of NAD(H) and NADP(H)

Molecular properties, functions, and potential applications of NAD kinases

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